Regulation of NMDA glutamate receptor functions by the GluN2 subunits
Open accessAbstract
The N‐methyl‐D‐aspartate receptors (NMDARs) are ionotropic glutamate receptors that mediate the flux of calcium (Ca 2+) into the post‐synaptic compartment. Ca 2+ influx subsequently triggers the activation of various intracellular signalling cascades that underpin multiple forms of synaptic plasticity. Functional NMDARs are assembled as heterotetramers composed of two obligatory GluN1 subunits and two GluN2 or GluN3 subunits. Four different GluN2 subunits (GluN2A‐D) are present throughout the central nervous system; however, they are differentially expressed, both developmentally and spatially, in a cell‐ and synapse‐specific manner. Each GluN2 subunit confers NMDARs with distinct ion channel properties and intracellular trafficking pathways. Regulated membrane trafficking of NMDARs is a dynamic process that ultimately determines the number of NMDARs at synapses, and is controlled by subunit‐specific interactions with various intracellular regulatory proteins. Here we review recent progress made towards understanding the molecular mechanisms that regulate the trafficking of GluN2‐containing NMDARs, focusing on the roles of several key synaptic proteins that interact with NMDARs via their carboxyl termini. image
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Specific GluN2 subunits confer distinct ion channel properties and intracellular trafficking pathways, and their expression patterns vary developmentally and spatially across the central nervous system.
“The specific GluN2 subunits confer distinct ion channel properties and intracellular trafficking pathways, and their expression patterns vary developmentally and spatially across the central nervous system [48] (Figure 3).”
From Molecular Physiology of the Neuronal Synapse (2026) · cites this paper as [48]
NMDARs are crucial for synaptic plasticity and memory formation, functioning as coincidence detectors that require both presynaptic glutamate release and postsynaptic depolarization to open their ion channel and allow calcium influx.
“NMDARs are crucial for synaptic plasticity and memory formation, functioning as “coincidence detectors” that require both presynaptic glutamate release and postsynaptic depolarization to open their ion channel and allow for calcium influx [48].”
From Molecular Physiology of the Neuronal Synapse (2026) · cites this paper as [48]
NMDARs are not a homogeneous group.
“The distinct biophysical properties and spatiotemporal expression patterns of different GluN2 subunits emphasize that NMDARs are not a homogeneous group [48].”
From Molecular Physiology of the Neuronal Synapse (2026) · cites this paper as [48]
NMDAR trafficking is a complex process involving biosynthesis, dendritic transport, exocytosis, lateral diffusion, endocytosis, recycling, and degradation, all tightly controlled by protein-protein interactions involving the cytoplasmic carboxyl termini of NMDAR subunits.
“NMDAR trafficking is a complex process involving biosynthesis, dendritic transport, exocytosis, lateral diffusion, endocytosis, recycling, and degradation, all tightly controlled by protein–protein interactions involving the cytoplasmic carboxyl termini (CTDs) of NMDAR subunits [48].”
From Molecular Physiology of the Neuronal Synapse (2026) · cites this paper as [48]
GluN2B-containing NMDARs are generally more mobile than GluN2A-containing receptors, which tend to be more stably localized at synapses.
“GluN2B-containing NMDARs are generally more mobile than GluN2A-containing receptors, which tend to be more stably localized at synapses.”
From Molecular Physiology of the Neuronal Synapse (2026) · cites this paper as [48]
The GluN2B-to-GluN2A subunit switch alters NMDAR-mediated calcium influx, thereby impacting dendritic integration and synaptic plasticity rules.
“This subunit switch profoundly alters NMDAR-mediated calcium influx, thereby impacting dendritic integration and synaptic plasticity rules [48].”
From Molecular Physiology of the Neuronal Synapse (2026) · cites this paper as [48]
Functional NMDARs are heterotetramers composed of two obligatory GluN1 subunits and two GluN2 (GluN2A-D) or GluN3 subunits.
“Functional NMDARs are heterotetramers composed of two obligatory GluN1 subunits and two GluN2 (GluN2A-D) or GluN3 subunits.”
From Molecular Physiology of the Neuronal Synapse (2026) · cites this paper as [48]
NMDARs exhibit lateral diffusion on the plasma membrane, moving between synaptic and extrasynaptic sites.
“NMDARs exhibit lateral diffusion on the plasma membrane, moving between synaptic and extrasynaptic sites [48].”
From Molecular Physiology of the Neuronal Synapse (2026) · cites this paper as [48]
NMDAR endocytosis is primarily clathrin-mediated and involves the adaptor protein-2 (AP-2) complex.
“NMDAR endocytosis is primarily clathrin-mediated and involves the adaptor protein-2 (AP-2) complex [48].”
From Molecular Physiology of the Neuronal Synapse (2026) · cites this paper as [48]
DAPK1 functions as a refined physiological regulator during LTD, where its recruitment to GluN2B prevents CaMKII accumulation in the spine, thereby enabling bidirectional control of synaptic strength.
“Beyond its pathological role in excitotoxicity, DAPK1 functions as a refined physiological regulator during long-term depression (LTD), where its recruitment to GluN2B prevents CaMKII accumulation in the spine, thereby enabling bidirectional control of synaptic strength [48,54].”
From Molecular Physiology of the Neuronal Synapse (2026) · cites this paper as [48]
Sorting Nexin 27 (SNX27) is implicated in regulating NMDAR recycling from endosomes back to the plasma membrane.
“Sorting Nexin 27 (SNX27) is also implicated in regulating NMDAR recycling from endosomes back to the plasma membrane [48,50].”
From Molecular Physiology of the Neuronal Synapse (2026) · cites this paper as [48]
In the context of excitotoxicity, DAPK1 is recruited to extrasynaptic GluN2B-containing NMDARs.
“In the context of excitotoxicity, particularly relevant in neurological disorders, death-associated protein kinase 1 (DAPK1) is recruited to extrasynaptic GluN2B-containing NMDARs [48].”
From Molecular Physiology of the Neuronal Synapse (2026) · cites this paper as [48]
DAPK1 plays a role in LTD, where its activation via calcineurin-dependent dephosphorylation leads to GluN2B phosphorylation at Ser-1303, strengthening DAPK1 interaction and preventing CaMKII binding.
“DAPK1 also plays a role in LTD, where its activation via calcineurin-dependent dephosphorylation leads to GluN2B phosphorylation at Ser-1303, strengthening DAPK1 interaction and preventing CaMKII binding.”
From Molecular Physiology of the Neuronal Synapse (2026) · cites this paper as [48]
GluN2B-containing receptors show higher internalization rates in mature neurons, with their internalization modulated by phosphorylation of Tyr-1472 by Fyn kinase.
“GluN2B-containing receptors show higher internalization rates in mature neurons, with their internalization modulated by phosphorylation of Tyr-1472 by Fyn kinase.”
From Molecular Physiology of the Neuronal Synapse (2026) · cites this paper as [48]
CaMKII phosphorylates GluN2B at Ser-1303, which can reduce its own binding and increase surface GluN2B expression.
“CaMKII also phosphorylates GluN2B at Ser-1303, which can reduce its own binding and increase surface GluN2B expression [48].”
From Molecular Physiology of the Neuronal Synapse (2026) · cites this paper as [48]
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“…Ca2+ influx through the extrasynaptic GluN2B-containing receptors, in the context of both acute and chronic neurological disorders including ischaemic stroke and Alzheimer's disease is well-established (Hardingham, Fukunaga, & Bading, 2002; Martel, Ryan, & Bell, 2012; Parsons & Raymond, 2014).”
Background15q13.3 microdeletions increase risk of idiopathic generalized epilepsy.
Helbig, I., Mefford, H. C., Sharp, A. J., Guipponi, M., Fichera, M., Franke, A., Muhle, H., de Kovel, C., Baker, C., von Spiczak, S., et al. (2009) · Nature Genetics · doi:10.1038/ng.292 · Cited by 551 · see citing works
Molecular determinants of NMDA receptor internalization
Roche, K. W., Standley, S., McCallum, J., Dune Ly, C., Ehlers, M. D., & Wenthold, R. J. (2001) · Nature Neuroscience · doi:10.1038/90498 · Cited by 550 · cited 7× · see citing works
“This mechanism generally involves clathrincoated pits, which occur laterally relative to the PSD (Petralia, Wang, & Wenthold, 2003; Blanpied, Scott, & Ehlers, 2002), and require the adaptor protein-2 (AP-2) complex (Racz, Blanpied, Ehlers, & Weinberg, 2004; Lavezzari, McCallum, Dewey, & Roche, 2004; Roche et al., 2001…”
BackgroundInfluentialSelf-citationA developmental change in NMDA receptor-associated proteins at hippocampal synapses
Sans, N., Petralia, R. S., Wang, Y.-X., Blahos, J., Hell, J. W., & Wenthold, R. J. (2000) · The Journal of Neuroscience · doi:10.1523/jneurosci.20-03-01260.2000 · Cited by 537 · cited 7× · see citing works
“Interestingly, SAP102 is localized not only at synapses, but also in the cytoplasm and ER (Sans et al., 2000).”
BackgroundInfluentialSubunit-Specific NMDA Receptor Trafficking to Synapses
Barria, A., & Malinow, R. (2002) · Neuron · doi:10.1016/s0896-6273(02)00776-6 · Cited by 515 · cited 3× · see citing works
“During development, synapses possess GluN2B-containing NMDARs (Aizenman & Cline, 2007; Barria & Malinow, 2002) but no functional AMPARs, rendering them silent (Isaac, Nicoll, & Malenka, 1995; Isaac, Crair, Nicoll, & Malenka, 1997; Liao, Hessler, & Malinow, 1995).”
BackgroundSilent synapses during development of thalamocortical inputs
Isaac, J. T. R., Crair, M. C., Nicoll, R. A., & Malenka, R. C. (1997) · Neuron · doi:10.1016/s0896-6273(00)80267-6 · Cited by 507 · see citing works
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DAPK1 Interaction with NMDA Receptor NR2B Subunits Mediates Brain Damage in Stroke
Tu, W., Xu, X., Peng, L., Zhong, X., Zhang, W., Soundarapandian, M. M., Belal, C., Wang, M., Jia, N., Zhang, W., et al. (2010) · Cell · doi:10.1016/j.cell.2009.12.055 · Cited by 493 · cited 1× · see citing works
“DAPK1 directly interacts with the GluN2B CTD in a region that overlaps with the CaMKII-binding site (Tu et al., 2010).”
BackgroundAkazawa, C., Shigemoto, R., Bessho, Y., Nakanishi, S., & Mizuno, N. (1994) · The Journal of comparative neurology · doi:10.1002/cne.903470112 · Cited by 490 · see citing works
Strack, S., & Colbran, R. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.33.20689 · Cited by 466 · cited 1× · see citing works
“One of the major interacting partners for CaMKII is the GluN2B subunit of NMDARs (Bayer et al., 2001; Leonard, Lim, Hemsworth, Horne, & Hell, 1999; Leonard et al., 2002; Strack & Colbran, 1998).”
BackgroundImportance of the Intracellular Domain of NR2 Subunits for NMDA Receptor Function In Vivo
Sprengel, R., Suchanek, B., Amico, C., Brusa, R., Burnashev, N., Rozov, A. V., Hvalby, Ø., Jensen, V., Paulsen, O., Andersen, P. N., et al. (1998) · Cell · doi:10.1016/s0092-8674(00)80921-6 · Cited by 460 · cited 4× · see citing works
“GluN2AΔC/ΔC mice show severe reductions in synaptic GluN2A expression and NMDAR-mediated EPSCs, as well as impairments in LTP and contextual memory (Sprengel et al., 1998; Steigerwald et al., 2000).”
BackgroundInfluentialTreatment of stroke with a PSD-95 inhibitor in the gyrencephalic primate brain
Cook, D. J., Teves, L. M., & Tymianski, M. (2012) · Nature · doi:10.1038/nature10841 · Cited by 446 · see citing works
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SAP102, a novel postsynaptic protein that interacts with NMDA receptor complexes in vivo.
Müller, B., Kistner, U., Kindler, S., Chung, W. J., Kuhlendahl, S., Fenster, S. D., Lau, L.-F., Veh, R., Huganir, R., Gundelfinger, E., et al. (1996) · Neuron · doi:10.1016/s0896-6273(00)80157-9 · Cited by 435 · cited 1× · see citing works
“Other MAGUK family members, including SAP102, SAP97 and PSD-93 were subsequently shown to interact with the C-terminal type I PDZ-binding motif (-ES[D/E]V) in the GluN2 subunits of NMDARs (Muller et al., 1996; Niethammer et al., 1996; Kim, Cho, Rothschild, & Sheng, 1996).”
BackgroundRetromer: A Master Conductor of Endosome Sorting
Burd, C., & Cullen, P. J. (2014) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a016774 · Cited by 435 · see citing works
Glycine binding primes NMDA receptor internalization
Nong, Y., Huang, Y.-Q., Ju, W., Kalia, L. V., Ahmadian, G., Wang, Y.-T., & Salter, M. (2003) · Nature · doi:10.1038/nature01497 · Cited by 434 · cited 1× · see citing works
“Notably, glycine conditioning promotes receptor endocytosis by increasing the interaction with the endocytic AP-2 complex, thereby priming NMDARs for internalization upon receptor activation (Nong et al., 2003).”
BackgroundLesca, G., Rudolf, G., Bruneau, N., Lozovaya, N., Labalme, A., Boutry‐Kryza, N., Salmi, M., Tsintsadze, T. S., Addis, L., Motte, J. E., et al. (2013) · Nature Genetics · doi:10.1038/ng.2726 · Cited by 433 · see citing works
The NMDA Receptor Is Coupled to the ERK Pathway by a Direct Interaction between NR2B and RasGRF1
Krapivinsky, G. B., Krapivinsky, L., Manasian, Y., Ivanov, A., Tyzio, R., Pellegrino, C., Ben‐Ari, Y., Clapham, D. E., & Medina, I. (2003) · Neuron · doi:10.1016/s0896-6273(03)00645-7 · Cited by 431 · see citing works
Differential activity-dependent regulation of the lateral mobilities of AMPA and NMDA receptors
Groc, L., Heine, M., Cognet, L., Brickley, K., Stephenson, F. A., Lounis, B., & Choquet, D. (2004) · Nature Neuroscience · doi:10.1038/nn1270 · Cited by 429 · cited 2× · see citing works
“Lateral mobilities of synaptic AMPAand NMDA-Rs are comparable, whereas extrasynaptic AMPARs are more mobile than NMDARs (Groc et al., 2004).”
BackgroundMobile NMDA Receptors at Hippocampal Synapses
Tovar, K. R., & Westbrook, G. L. (2002) · Neuron · doi:10.1016/s0896-6273(02)00658-x · Cited by 428 · see citing works
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Long-Term Potentiation: From CaMKII to AMPA Receptor Trafficking
Herring, B. E., & Nicoll, R. A. (2016) · Annual Review of Physiology · doi:10.1146/annurev-physiol-021014-071753 · Cited by 425 · cited 1× · see citing works
“CaMKII is a multi-subunit protein kinase comprising 12 catalytically active subunits that is crucial for synaptic plasticity, learning and memory (Herring & Nicoll, 2016; Lisman et al., 2012; Hell, 2014).”
BackgroundA de novo convergence of autism genetics and molecular neuroscience
Krumm, N., O’Roak, B. J., Shendure, J., & Eichler, E. E. (2014) · Trends in Neurosciences · doi:10.1016/j.tins.2013.11.005 · Cited by 423 · cited 1× · see citing works
“Among these, a cluster of synapse-associated genes have been identified (Gilman et al., 2011; Glessner, Wang, & Cai, 2009; Krumm et al., 2014), which includes genes that encode various NMDAR subunits (De Rubeis, He, & Goldberg, 2014; Sanders, He, & Willsey, 2015).”
BackgroundProtein kinase C modulates NMDA receptor trafficking and gating
Lan, J.-Y., Skeberdis, V. A., Jover, T., Grooms, S. Y., Lin, Y., Araneda, R. C., Zheng, X., Bennett, M. V. L., & Zukin, R. S. (2001) · Nature Neuroscience · doi:10.1038/86028 · Cited by 421 · see citing works
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An NMDA receptor ER retention signal regulated by phosphorylation and alternative splicing
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“Genetic deletion or shRNA-mediated knockdown of PSD-95 results in the fragmentation of the PSD and a patchy loss of synaptic AMPARs, but not NMDARs (Chen, Nelson, & Li, 2011; Beique et al., 2006; Elias et al., 2006).”
BackgroundInfluentialHill, M. D., Martin, R., Mikulis, D. J., Wong, J. H., Silver, F. L., terBrugge, K. G., Milot, G., Clark, W. M., Macdonald, R. L., Kelly, M., et al. (2012) · The Lancet Neurology · doi:10.1016/s1474-4422(12)70225-9 · Cited by 403 · see citing works
Synapse-specific regulation of AMPA receptor function by PSD-95.
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“05.033 Beique, J. C., Lin, D. T., Kang, M. G., Aizawa, H., Takamiya, K., & Huganir, R. L. (2006).”
InfluentialDiversity in NMDA Receptor Composition
Sanz-Clemente, A., Nicoll, R. A., & Roche, K. W. (2012) · The Neuroscientist · doi:10.1177/1073858411435129 · Cited by 397 · see citing works
Self-citationRegulation of NMDA receptors by phosphorylation.
Chen, B.-S., & Roche, K. (2007) · Neuropharmacology · doi:10.1016/j.neuropharm.2007.05.018 · Cited by 394 · cited 1× · see citing works
“In addition to the modulatory role of post-translational modifications in surface expression (Chen & Roche, 2007; Lussier et al., 2015), several scaffolding proteins have been identified as NMDAR regulators.”
BackgroundSelf-citationLeonard, A. S., Lim, I. A., Hemsworth, D. E., Horne, M. C., & Hell, J. W. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.6.3239 · Cited by 385 · see citing works
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“…phosphorylation of Ser-1480, which lies on the PDZbinding domain of GluN2B has the opposite effect, contributing to increased internalization of the receptor (Lavezzari et al., 2003; Prybylowski et al., 2005) because of impaired binding to MAGUK proteins (Chung, Huang, Lau, & Huganir, 2004).”
BackgroundNMDA receptor surface mobility depends on NR2A-2B subunits
Groc, L., Heine, M., Cousins, S. L., Stephenson, F. A., Lounis, B., Cognet, L., & Choquet, D. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0605238103 · Cited by 376 · cited 1× · see citing works
“There are several lines of evidence supporting the notion that extrasynaptically located GluN2B-containing NMDARs are more mobile than GluN2A, which remains more synaptically localized (Groc et al., 2006; Dupuis et al., 2014; Ferreira, Papouin, & Ladepeche, 2017; Kellermayer et al., 2018).”
BackgroundGRIN2A mutations cause epilepsy-aphasia spectrum disorders
Carvill, G. L., Regan, B. M., Yendle, S. C., O’Roak, B. J., Lozovaya, N., Bruneau, N., Burnashev, N., Khan, A., Cook, J., Geraghty, E., et al. (2013) · Nature Genetics · doi:10.1038/ng.2727 · Cited by 375 · see citing works
Metabotropic Glutamate Receptors
Dillon, J., Franks, C., Murray, C., Edwards, R. J., Calahorro, F., Ishihara, T., Katsura, I., Holden-Dye, L., & O'Connor, V. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.606608 · Cited by 367
Dynamics and Regulation of Clathrin Coats at Specialized Endocytic Zones of Dendrites and Spines
Blanpied, T. A., Scott, D. B., & Ehlers, M. (2002) · Neuron · doi:10.1016/s0896-6273(02)00979-0 · Cited by 366 · see citing works
Rapid bidirectional switching of synaptic NMDA receptors.
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“A rapid switching (in minutes) of GluN2B- to GluN2A-containing NMDARs can be induced by an LTP inducing protocol in acute hippocampal slices from young animals (Bellone & Nicoll, 2007).”
BackgroundStrack, S., McNeill, R. B., & Colbran, R. J. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m001471200 · Cited by 356 · see citing works
CaMKII: Claiming Center Stage in Postsynaptic Function and Organization
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“CaMKII is a multi-subunit protein kinase comprising 12 catalytically active subunits that is crucial for synaptic plasticity, learning and memory (Herring & Nicoll, 2016; Lisman et al., 2012; Hell, 2014).”
BackgroundHamdan, F. F., Gauthier, J., Araki, Y., Lin, D.-T., Yoshizawa, Y., Higashi, K., Park, A.-R., Spiegelman, D., Dobrzeniecka, S., Piton, A., et al. (2011) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2011.02.001 · Cited by 349 · see citing works
PDZ Domain Suppression of an ER Retention Signal in NMDA Receptor NR1 Splice Variants
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Self-citationDisrupted surface cross-talk between NMDA and Ephrin-B2 receptors in anti-NMDA encephalitis
Mikasova, L., De Rossi, P., Bouchet, D., Georges, F., Rogemond, V., Didelot, A., Meissirel, C., Honnorat, J., & Groc, L. (2012) · Brain · doi:10.1093/brain/aws092 · Cited by 341 · cited 2× · see citing works
“, 2009), secreted proteases (Lesept, Chevilley, & Jezequel, 2016), growth factors (De Rossi, Harde, & Dupuis, 2016), cell surface receptors (Ladepeche et al., 2013; Mikasova et al., 2012) and hormones (Potier et al.”
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NMDA receptor trafficking through an interaction between PDZ proteins and the exocyst complex
Sans, N., Prybylowski, K., Petralia, R. S., Chang, K., Wang, Y.-X., Racca, C., Vicini, S., & Wenthold, R. J. (2003) · Nature Cell Biology · doi:10.1038/ncb990 · Cited by 327 · cited 18× · see citing works
“SAP97 phosphorylation at Ser-39 drives the translocation of SAP97 from the ER to the post-synaptic compartment, whereas its phosphorylation at Ser-232 disrupts SAP97 interaction with GluN2A.”
BackgroundInfluentialFritschy, J., Weinmann, O., Wenzel, A., & Benke, D. (1998) · The Journal of Comparative Neurology · doi:10.1002/(sici)1096-9861(19980112)390:2 · Cited by 321 · see citing works
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“…its interaction with MAGUKs, which results in lateral diffusion of GluN2B to extrasynaptic sites and the internalization of NMDARs through a coordinated dephosphorylation of Tyr-1472 within the endocytic motif (Sanz-Clemente et al., 2010, Sanz-Clemente, Gray et al. 2013; Chung et al., 2004).”
BackgroundTymianski, M., & Tator, C. H. (1996) · Neurosurgery · doi:10.1097/00006123-199606000-00028 · Cited by 312 · cited 1× · see citing works
“…Ca2+-dependent processes that trigger the initiation of cell death mechanisms and ensuing neurodegeneration in various brain regions (Arundine & Tymianski, 2003; Choi, 1988; Mehta, Prabhakar, Kumar, Deshmukh, & Sharma, 2013; Tymianski & Tator, 1996; Ong, Tanaka, Dawe, Ittner, & Farooqui, 2013).”
BackgroundChen, X., Levy, J. M., Hou, A., Winters, C., Azzam, R., Sousa, A. A., Leapman, R. D., Nicoll, R. A., & Reese, T. S. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1517045112 · Cited by 310 · cited 2× · see citing works
“However, simultaneous down-regulation of two (PSD-95 and PSD-93) or three (PSD-95, PSD-93 and SAP102) MAGUKs causes a profound loss of functional synaptic glutamate receptors because of disintegration of the PSD structure (Elias et al., 2006; Chen et al., 2015; Levy, Chen, Reese, & Nicoll, 2015).”
BackgroundCalcium/calmodulin-dependent protein kinase II and synaptic plasticity
Colbran, R. J., & Brown, A. M. (2004) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2004.05.008 · Cited by 307 · cited 1× · see citing works
“This autophosphorylation allows the activity of CaMKII to persist long after the removal of Ca2+ and calmodulin in the PSD (Colbran & Brown, 2004; Bayer & Schulman, 2019).”
BackgroundCaM Kinase: Still Inspiring at 40
Bayer, K. U., & Schulman, H. (2019) · Neuron · doi:10.1016/j.neuron.2019.05.033 · Cited by 307 · cited 1× · see citing works
“This autophosphorylation allows the activity of CaMKII to persist long after the removal of Ca2+ and calmodulin in the PSD (Colbran & Brown, 2004; Bayer & Schulman, 2019).”
BackgroundOmkumar, R. V., Kiely, M. J., Rosenstein, A. J., Min, K.-T., & Kennedy, M. B. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.49.31670 · Cited by 304 · see citing works
Linking early-life NMDAR hypofunction and oxidative stress in schizophrenia pathogenesis
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“In accordance, there is a significant overlap in genes associated with ASDs, intellectual disability, epilepsy and schizophrenia (Hardingham & Do, 2016; Helbig, Mefford, & Sharp, 2009; International Schizophrenia 2008; Miller, Shen, & Weiss, 2009; Sharp, Mefford, & Li, 2008; Stefansson, Rujescu, &…”
PSD-95 Is Required to Sustain the Molecular Organization of the Postsynaptic Density
Chen, X., Nelson, C. D., Li, X., Winters, C. A., Azzam, R. N., Sousa, A. A., Leapman, R. D., Gainer, H., Sheng, M., & Reese, T. S. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.5968-10.2011 · Cited by 304 · see citing works
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Syntaxin-4 defines a domain for activity-dependent exocytosis in dendritic spines
Kennedy, M. J., Davison, I. G., Robinson, C. G., & Ehlers, M. D. (2010) · Cell · doi:10.1016/j.cell.2010.02.042 · Cited by 294 · see citing works
Xu, J., Kurup, P., Zhang, Y., Goebel-Goody, S., Wu, P. H., Hawasli, A. H., Baum, M., Bibb, J., & Lombroso, P. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.2212-09.2009 · Cited by 293 · cited 1× · see citing works
“Extrasynaptic NMDARs also induce the activation of deleterious proteins, such as calpains (Xu et al., 2009).”
BackgroundNMDA receptors in nervous system diseases
Zhou, Q., & Sheng, M. (2013) · Neuropharmacology · doi:10.1016/j.neuropharm.2013.03.030 · Cited by 293 · cited 1× · see citing works
“NMDAR dysfunction has long been thought to have a paramount role in a variety of neurological disorders, ranging from acute (e.g. stroke and global cerebral ischaemia) to chronic disorders such as Alzheimer's or Huntington's disease (Zhou & Sheng, 2013; Ittner & Gotz, 2011).”
BackgroundOrganization of the core structure of the postsynaptic density
Chen, X., Winters, C. A., Azzam, R. N., Li, X., Galbraith, J. A., Leapman, R. D., & Reese, T. S. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0800897105 · Cited by 290 · cited 1× · see citing works
“At the ultrastructural level, PSD-95 appears as vertically oriented filaments that anchor both AMPA- and NMDARs at the PSD (Chen et al., 2008).”
BackgroundMechanism of Ca2+/calmodulin-dependent kinase II regulation of AMPA receptor gating
Kristensen, A. S., Jenkins, M. A., Banke, T. G., Schousboe, A., Makino, Y., Johnson, R. C., Huganir, R., & Traynelis, S. F. (2011) · Nature Neuroscience · doi:10.1038/nn.2804 · Cited by 286 · cited 1× · see citing works
“…synaptic potentiation is associated with the phosphorylation and insertion of AMPARs into the synapses (Hayashi et al., 2000; Lee, Takamiya, & Han, 2003), as well as through an enhancement in AMPAR single-channel conductance (Derkach, Barria, & Soderling, 1999; Kristensen et al., 2011).”
BackgroundTeasdale, R. D., & Collins, B. M. (2011) · Biochemical Journal · doi:10.1042/bj20111226 · Cited by 282 · cited 1× · see citing works
“Sorting nexin 27, which contains an N-terminal PDZ domain, a lipidbinding PX domain and three C-terminal FERM (4.1N/ezrin/radixin/ moesin) domains, is a highly conserved regulator of cargo recycling from endosomes to the plasma membrane (Teasdale & Collins, 2012).”
BackgroundCalmodulin Mediates Calcium-Dependent Inactivation of N-Methyl-D-Aspartate Receptors
Zhang, S., Ehlers, M., Bernhardt, J. P., Su, C.-T., & Huganir, R. L. (1998) · Neuron · doi:10.1016/s0896-6273(00)80553-x · Cited by 278 · see citing works
Rauner, C., & Köhr, G. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.182600 · Cited by 270 · cited 1× · see citing works
“…and two different GluN2 subunits in many brain regions and neuronal types, such as GluN1/2A/2B, GluN1/2A/2C and GluN1/2B/2D complexes (Figure 1c) (Rauner & Kohr, 2011; Tovar, McGinley, & Westbrook, 2013; Luo, Wang, Yasuda, Dunah, & Wolfe, 1997; Brickley, Misra, Mok, Mishina, & Cull-Candy, 2003;…”
Influence of GluN2 subunit identity on NMDA receptor function
Wyllie, D. J. A., Livesey, M. R., & Hardingham, G. E. (2013) · Neuropharmacology · doi:10.1016/j.neuropharm.2013.01.016 · Cited by 260 · cited 1× · see citing works
“A long-standing debate in the field concerns the differential contribution of GluN2A- and GluN2B-containing NMDARs to excitotoxic neuronal death (Wyllie et al., 2013).”
BackgroundSubunit-Specific Regulation of NMDA Receptor Endocytosis
Lavezzari, G., McCallum, J. D., Dewey, C. M., & Roche, K. W. (2004) · Journal of Neuroscience · doi:10.1523/jneurosci.1890-04.2004 · Cited by 244 · cited 5× · see citing works
“Interaction with PSD-95 contributes to the stabilization of both GluN2 subunits at the cell surface, thereby reducing their rate of endocytosis (Lavezzari et al., 2004, 2003; Roche et al., 2001).”
BackgroundInfluentialSelf-citationCaMKII binding to GluN2B is critical during memory consolidation
Halt, A. R., Dallapiazza, R. F., Zhou, Y., Stein, I. S., Qian, H., Juntti, S., Wojcik, S., Brose, N., Silva, A. J., & Hell, J. W. (2012) · The EMBO Journal · doi:10.1038/emboj.2011.482 · Cited by 243 · see citing works
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“…SNX27 leads to a profound decrease in surface expression of AMPA- and NMDA-Rs; and, as a consequence, SNX27 knockout mice display deficits in LTP and behavioural abnormalities (Wang et al., 2013; Hussain, Diering, Sole, Anggono, & Huganir, 2014; Loo, Tang, Al-Haddawi, Stewart Dawe, & Hong, 2014).”
BackgroundMcGee, A. W., Dakoji, S., Olsen, O., Bredt, D. S., Lim, W. A., & Prehoda, K. E. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00411-7 · Cited by 239 · cited 1× · see citing works
“These MAGUKs are defined by the presence of three conserved PDZ domains, one SH3 domain followed by a catalytically inactive GK modular domain (Long et al., 2003; McGee et al., 2001; Doyle et al., 1996).”
BackgroundKrupp, J., Vissel, B., Thomas, C. G., Heinemann, S. F., & Westbrook, G. L. (1999) · Journal of Neuroscience · doi:10.1523/jneurosci.19-04-01165.1999 · Cited by 237 · see citing works
Mass of the postsynaptic density and enumeration of three key molecules
Chen, X., Vinade, L., Leapman, R. D., Petersen, J. D., Nakagawa, T., Phillips, T. M., Sheng, M., & Reese, T. S. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0505359102 · Cited by 236 · cited 1× · see citing works
“It is composed of mainly the α and β isoforms, is enriched in the PSD, and is one of the most abundant proteins in the brain (Chen et al., 2005).”
BackgroundLTP Requires a Unique Postsynaptic SNARE Fusion Machinery
Jurado, S., Goswami, D., Zhang, Y., Molina, A. J. M., Südhof, T. C., & Malenka, R. C. (2013) · Neuron · doi:10.1016/j.neuron.2012.11.029 · Cited by 232 · cited 1× · see citing works
“Consistent with this, shRNA-mediated knockdown of SNAP25 reduces NMDAR-mediated transmission in the hippocampus (Jurado et al., 2013).”
BackgroundHuman GRIN2B variants in neurodevelopmental disorders
Hu, C., Chen, W., Myers, S. J., Yuan, H., & Traynelis, S. F. (2016) · Journal of Pharmacological Sciences · doi:10.1016/j.jphs.2016.10.002 · Cited by 230 · cited 1× · see citing works
“Many of these mutations have been reviewed in detail elsewhere (Burnashev & Szepetowski, 2015; Hu et al., 2016), but new variants are still being identified.”
BackgroundLateral organization of endocytic machinery in dendritic spines
Rácz, B., Blanpied, T. A., Ehlers, M., & Weinberg, R. J. (2004) · Nature Neuroscience · doi:10.1038/nn1303 · Cited by 227 · see citing works
Casein Kinase 2 Regulates the NR2 Subunit Composition of Synaptic NMDA Receptors
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“, 2001) and alters the expression of synaptic GluN2A and GluN2B receptors (Sanz-Clemente et al., 2010).”
BackgroundSelf-citationElias, G. M., Elias, L. A. B., Apostolides, P. F., Kriegstein, A. R., & Nicoll, R. A. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0811025106 · Cited by 223 · cited 3× · see citing works
“…early development reduces both AMPAR- and NMDAR-mediated post-synaptic currents, whereas mice lacking PSD-95/PSD-93 fail to undergo the subunit switch from GluN2B to GluN2A (Elias et al., 2008), highlighting the role of PSD-95 and SAP102 at distinct developmental stages of excitatory synapses.”
BackgroundCui, H., Hayashi, A., Sun, H.-S., Belmares, M., Cobey, C., Phan, T., Schweizer, J., Salter, M., Wang, Y.-T., Tasker, R., et al. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.1464-07.2007 · Cited by 222 · see citing works
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“STEP61 is known to dephosphorylate GluN2B at Tyr-1472, which is part of the YEKL endocytic motif, and induces the internalization of GluN2B (Snyder, Nong, & Almeida, 2005; Kurup et al., 2010).”
BackgroundSAP97 and CASK mediate sorting of NMDA receptors through a previously unknown secretory pathway
Jeyifous, O., Waites, C. L., Specht, C. G., Fujisawa, S., Schubert, M., Lin, E. I., Marshall, J. J., Aoki, C. J., de Silva, T., Montgomery, J. M., et al. (2009) · Nature Neuroscience · doi:10.1038/nn.2362 · Cited by 219 · cited 2× · see citing works
“76 μm/s) as they contain large protein complexes containing the scaffolding molecules SAP97, CASK (mLin2), X11/Mint1 (mLin10) and mLin7 (MALS/Velis) that couple GluN2B to the motor protein KIF17 and facilitate the long-range transport of NMDAR-containing vesicles on microtubules along dendrites (Jeyifous et al., 2009;…”
BackgroundDual Palmitoylation of NR2 Subunits Regulates NMDA Receptor Trafficking
Hayashi, T., Thomas, G. M., & Huganir, R. L. (2009) · Neuron · doi:10.1016/j.neuron.2009.08.017 · Cited by 218 · cited 5× · see citing works
“STEP61 is known to dephosphorylate GluN2B at Tyr-1472, which is part of the YEKL endocytic motif, and induces the internalization of GluN2B (Snyder, Nong, & Almeida, 2005; Kurup et al., 2010).”
BackgroundInfluentialKIF17 Dynamics and Regulation of NR2B Trafficking in Hippocampal Neurons
Guillaud, L., Setou, M., & Hirokawa, N. (2003) · Journal of Neuroscience · doi:10.1523/jneurosci.23-01-00131.2003 · Cited by 213 · see citing works
NMDA Receptors in the Central Nervous System
Hansen, K. B., Yi, F., Perszyk, R. E., Menniti, F. S., & Traynelis, S. F. (2017) · Methods in molecular biology · doi:10.1007/978-1-4939-7321-7_1 · Cited by 206 · see citing works
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“GluN2AΔC/ΔC mice show severe reductions in synaptic GluN2A expression and NMDAR-mediated EPSCs, as well as impairments in LTP and contextual memory (Sprengel et al., 1998; Steigerwald et al., 2000).”
BackgroundMatrix Metalloproteinase-9 Controls NMDA Receptor Surface Diffusion through Integrin β1 Signaling
Michaluk, P., Mikasová, L., Groc, L., Frischknecht, R., Choquet, D., & Kaczmarek, L. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.5346-08.2009 · Cited by 204 · cited 1× · see citing works
“Other factors that are known to modulate NMDAR diffusion include the extracellular matrix (Michaluk et al., 2009), secreted proteases (Lesept, Chevilley, & Jezequel, 2016), growth factors (De Rossi, Harde, & Dupuis, 2016), cell surface receptors (Ladepeche et al., 2013; Mikasova et al., 2012) and…”
BackgroundIonotropic GABA and Glutamate Receptor Mutations and Human Neurologic Diseases
Yuan, H., Low, C., Moody, O. A., Jenkins, A., & Traynelis, S. F. (2015) · Molecular Pharmacology · doi:10.1124/mol.115.097998 · Cited by 202 · see citing works
Mechanisms underlying NMDA receptor synaptic/extrasynaptic distribution and function
Gladding, C. M., & Raymond, L. A. (2011) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2011.05.001 · Cited by 197 · cited 1× · see citing works
“In the adult forebrain, GluN2A-containing receptors are predominantly localized at synaptic sites, whereas GluN2B receptors are also found at the peri- or extrasynaptic sites (Bellone & Nicoll, 2007; Hardingham & Bading, 2010; Gladding & Raymond, 2011).”
BackgroundTriheteromeric NMDA Receptors at Hippocampal Synapses
Tovar, K., McGinley, M. J., & Westbrook, G. (2013) · Journal of Neuroscience · doi:10.1523/jneurosci.0829-13.2013 · Cited by 197 · see citing works
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NMDA receptor subunit mutations in neurodevelopmental disorders
Burnashev, N., & Szepetowski, P. (2014) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2014.11.008 · Cited by 194 · cited 1× · see citing works
“Many of these mutations have been reviewed in detail elsewhere (Burnashev & Szepetowski, 2015; Hu et al., 2016), but new variants are still being identified.”
BackgroundCoupling diverse routes of calcium entry to mitochondrial dysfunction and glutamate excitotoxicity
Stanika, R. I., Pivovarova, N. B., Brantner, C. A., Watts, C. A., Winters, C. A., & Andrews, S. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0903546106 · Cited by 191 · cited 2× · see citing works
“The most likely explanation, however, is that an interplay of factors beyond subunit composition, such as receptor localization, contributes to the decision between activation of pro-death versus pro-survival signalling pathways (Lai, Shyu, & Wang, 2011; Stanika et al., 2009; Zhou et al., 2013).”
BackgroundResultMatta, J. A., Ashby, M. C., Sanz-Clemente, A., Roche, K. W., & Isaac, J. T. R. (2011) · Neuron · doi:10.1016/j.neuron.2011.02.045 · Cited by 191 · see citing works
Self-citationKenny, E. M., Cormican, P., Furlong, S., Heron, E. A., Kenny, G., Fahey, C., Kelleher, E., Ennis, S., Tropea, D., Anney, R., et al. (2013) · Molecular Psychiatry · doi:10.1038/mp.2013.127 · Cited by 190 · see citing works
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Caldendrin–Jacob: A Protein Liaison That Couples NMDA Receptor Signalling to the Nucleus
Dieterich, D., Karpova, A., Mikhaylova, M., Zdobnova, I., König, I., Landwehr, M., Kreutz, M., Smalla, K., Richter, K., Landgraf, P., et al. (2008) · PLoS Biology · doi:10.1371/journal.pbio.0060034 · Cited by 182 · see citing works
Interactions between the NR2B Receptor and CaMKII Modulate Synaptic Plasticity and Spatial Learning
Zhou, Y., Takahashi, E., Li, W., Halt, A., Wiltgen, B., Ehninger, D., Li, G.-D., Hell, J. W., Kennedy, M. B., & Silva, A. J. (2007) · The Journal of Neuroscience · doi:10.1523/jneurosci.4486-07.2007 · Cited by 179 · see citing works
Mameli, M., Bellone, C., Brown, M. T. C., & Lüscher, C. (2011) · Nature Neuroscience · doi:10.1038/nn.2763 · Cited by 177 · see citing works
Stroke intervention pathways: NMDA receptors and beyond
Lai, T. W., Shyu, W., & Wang, Y. T. (2011) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2010.12.008 · Cited by 177 · see citing works
The Subtype of GluN2 C-terminal Domain Determines the Response to Excitotoxic Insults
Martel, M., Ryan, T. J., Bell, K. F. S., Fowler, J. H., McMahon, A., Al-Mubarak, B. R., Komiyama, N. H., Horsburgh, K. J., Kind, P. C., Grant, S. G. N., et al. (2012) · Neuron · doi:10.1016/j.neuron.2012.03.021 · Cited by 176 · cited 4× · see citing works
“A complementary experiment involving the GluN2B chimera containing the CTD of GluN2A produces the opposite effect, promoting neuronal survival (Cepeda & Levine, 2012; Martel et al., 2012; Vieira et al., 2016).”
BackgroundInfluentialSwanger, S. A., Chen, W., Wells, G., Burger, P. B., Tankovic, A., Bhattacharya, S., Strong, K. L., Hu, C., Kusumoto, H., Zhang, J., et al. (2016) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2016.10.002 · Cited by 176 · cited 1× · see citing works
“Indeed, variants identified in the agonist-binding domain (Swanger et al., 2016; Sceniak et al., 2019) or the channel forming regions (Ogden et al., 2011; Yuan, Hansen, & Zhang, 2014; Fedele et al., 2018; Vyklicky, Krausova, & Cerny, 2018) in both GRIN2A and GRIN2B are known to cause a wide…”
BackgroundLavezzari, G., McCallum, J. D., Lee, R., & Roche, K. W. (2003) · Neuropharmacology · doi:10.1016/s0028-3908(03)00308-3 · Cited by 173 · cited 3× · see citing works
“…phosphorylation of Ser-1480, which lies on the PDZbinding domain of GluN2B has the opposite effect, contributing to increased internalization of the receptor (Lavezzari et al., 2003; Prybylowski et al., 2005) because of impaired binding to MAGUK proteins (Chung, Huang, Lau, & Huganir, 2004).”
BackgroundSelf-citationIncontro, S., Díaz-Alonso, J., Iafrati, J., Vieira, M., Asensio, C. S., Sohal, V. S., Roche, K. W., Bender, K. J., & Nicoll, R. A. (2018) · Nature Communications · doi:10.1038/s41467-018-04439-7 · Cited by 171 · cited 4× · see citing works
“More recently, a role for CaMKIIα, but not CaMKIIβ, in controlling basal AMPAR and NMDAR neurotransmission has been reported (Incontro et al., 2018).”
BackgroundInfluentialSelf-citationCycling of NMDA Receptors during Trafficking in Neurons before Synapse Formation
Washbourne, P., Liu, X.-B., Jones, E. G., & McAllister, A. K. (2004) · Journal of Neuroscience · doi:10.1523/jneurosci.2555-04.2004 · Cited by 170 · see citing works
Frank, R., Komiyama, N. H., Ryan, T. J., Zhu, F., O’Dell, T. J., & Grant, S. G. N. (2016) · Nature Communications · doi:10.1038/ncomms11264 · Cited by 169 · cited 3× · see citing works
“5 mega-Dalton NMDAR-MAGUK supercomplexes in vivo (Frank et al., 2016; Frank & Grant, 2017).”
BackgroundInfluentialCoupling of extrasynaptic NMDA receptors to a CREB shut-off pathway is developmentally regulated
Hardingham, G. E., & Bading, H. (2002) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/s1570-9639(02)00455-7 · Cited by 168 · cited 1× · see citing works
“This effect is counteracted by activation of extrasynaptic NMDARs, which shuts-off CREB-dependent signalling (Dieterich, Karpova, & Mikhaylova, 2008; Hardingham & Bading, 2002; Hardingham et al., 2002; Karpova, Mikhaylova, & Bera, 2013).”
BackgroundAllosteric modulators of NMDA receptors: multiple sites and mechanisms
Zhu, S., & Paoletti, P. (2014) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2014.10.009 · Cited by 167 · cited 1× · see citing works
“…with differences in sensitivity to extracellular Zn2+, protons, spermine and other pharmacological agonists, antagonists and allosteric modulators, which are described in detail in several excellent reviews (Hansen et al., 2018; Traynelis et al., 2010; Zhu & Paoletti, 2015; Hackos & Hanson, 2017).”
BackgroundLussier, M. P., Sanz-Clemente, A., & Roche, K. W. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.r115.652750 · Cited by 163 · cited 2× · see citing works
“In addition to the modulatory role of post-translational modifications in surface expression (Chen & Roche, 2007; Lussier et al., 2015), several scaffolding proteins have been identified as NMDAR regulators.”
BackgroundSelf-citationBrickley, S. G., Misra, C., Mok, M. H. S., Mishina, M., & Cull-Candy, S. G. (2003) · Journal of Neuroscience · doi:10.1523/jneurosci.23-12-04958.2003 · Cited by 161 · cited 1× · see citing works
“Similarly, GluN2B and GluN2D are present in cerebellar Golgi cells despite their low expression in the cerebellum (Brickley et al., 2003).”
BackgroundMcIlhinney, R. A. J., Bourdellès, B. L., Molnár, E., Tricaud, N., Streit, P., & Whiting, P. (1998) · Neuropharmacology · doi:10.1016/s0028-3908(98)00121-x · Cited by 160 · cited 1× · see citing works
“Transfection of individual GluN2, and some GluN1 splice variants, results in retention in the ER unless assembled as GluN1/GluN2 tetramers (McIlhinney et al., 1998).”
BackgroundSpecific Targeting of Pro-Death NMDA Receptor Signals with Differing Reliance on the NR2B PDZ Ligand
Soriano, F. X., Martel, M., Papadia, S., Vaslin, A., Baxter, P. S., Rickman, C., Forder, J. P., Tymianski, M., Duncan, R. R., Aarts, M. M., et al. (2008) · Journal of Neuroscience · doi:10.1523/jneurosci.1207-08.2008 · Cited by 156 · see citing works
Relationship between Availability of NMDA Receptor Subunits and Their Expression at the Synapse
Prybylowski, K., Fu, Z., Losi, G., Hawkins, L. M., Luo, J.-H., Chang, K., Wenthold, R., & Vicini, S. (2002) · Journal of Neuroscience · doi:10.1523/jneurosci.22-20-08902.2002 · Cited by 156 · cited 1× · see citing works
“Over-expression of GluN2A and GluN2B in the cerebellar granule neurons significantly promote the number and synaptic targeting of NMDARs (Prybylowski et al., 2002).”
BackgroundMAGUKs: multifaceted synaptic organizers
Won, S., Levy, J. M., Nicoll, R. A., & Roche, K. W. (2017) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2017.01.006 · Cited by 155 · see citing works
Self-citationA neuronal role for SNAP-23 in postsynaptic glutamate receptor trafficking
Suh, Y. H., Terashima, A., Petralia, R. S., Wenthold, R. J., Isaac, J. T. R., Roche, K. W., & Roche, P. A. (2010) · Nature Neuroscience · doi:10.1038/nn.2488 · Cited by 153 · cited 2× · see citing works
“Genetic deletion of SNAP23 (SNAP23+/-) significantly reduces surface expression of endogenous GluN1, GluN2A and GluN2B subunits of NMDARs without affecting AMPAR levels (Suh et al., 2010).”
BackgroundResultSelf-citationA molecular code for endosomal recycling of phosphorylated cargos by the SNX27–retromer complex
Clairfeuille, T., Mas, C., Chan, A. S. M., Yang, Z., Tello‐Lafoz, M., Chandra, M., Widagdo, J., Kerr, M. C., Paul, B., Mérida, I., et al. (2016) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3290 · Cited by 150 · cited 5× · see citing works
“…Xiao, & Shaw, (2018) (Continues) subunits, and they may possess different regulatory signals that confer distinct binding affinities towards different MAGUK or other PDZ domain-containing proteins (Bard et al., 2010; Clairfeuille et al., 2016; Frank et al., 2016; Chen, Gray et al., 2012).”
BackgroundInfluentialSelf-citationZhou, X., Ding, Q., Chen, Z., Yun, H., & Wang, H. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.482000 · Cited by 148 · cited 1× · see citing works
“The most likely explanation, however, is that an interplay of factors beyond subunit composition, such as receptor localization, contributes to the decision between activation of pro-death versus pro-survival signalling pathways (Lai, Shyu, & Wang, 2011; Stanika et al., 2009; Zhou et al., 2013).”
BackgroundLong-term potentiation: Peeling the onion
Nicoll, R. A., & Roche, K. W. (2013) · Neuropharmacology · doi:10.1016/j.neuropharm.2013.02.010 · Cited by 146 · cited 1× · see citing works
“Upon heightened neuronal activity, such as during long-term potentiation (LTP), the Mg2+ blockade is relieved, leading to the opening of NMDARs that permit Ca2+ influx into the post-synaptic compartment (Nicoll & Roche, 2013).”
BackgroundSelf-citationMori, H., Manabe, T., Watanabe, M., Satoh, Y., Suzuki, N., Toki, S., Nakamura, K., Yagi, T., Kushiya, E., Takahashi, T., et al. (1998) · Neuron · doi:10.1016/s0896-6273(00)80567-x · Cited by 145 · cited 1× · see citing works
“Deletion of GluN2B CTD also reduces surface expression and synaptic retention of GluN2B receptors (Mori et al., 1998; Sprengel et al., 1998; Barria & Malinow, 2002; Mohrmann, Kohr, Hatt, Sprengel, & Gottmann, 2002).”
Triheteromeric NMDA receptors: from structure to synaptic physiology
Stroebel, D., Casado, M., & Paoletti, P. (2017) · Current Opinion in Physiology · doi:10.1016/j.cophys.2017.12.004 · Cited by 144 · see citing works
Kumar, S. S., & Huguenard, J. R. (2003) · Journal of Neuroscience · doi:10.1523/jneurosci.23-31-10074.2003 · Cited by 142 · cited 1× · see citing works
“In the layer 5 pyramidal neurons, GluN2A and GluN2B are differentially enriched at synapses of the callosal and the intracortical pathways respectively (Kumar & Huguenard, 2003).”
BackgroundMolecular bases of NMDA receptor subtype‐dependent properties
Glasgow, N. G., Retchless, B. S., & Johnson, J. W. (2014) · The Journal of Physiology · doi:10.1113/jphysiol.2014.273763 · Cited by 138 · see citing works
Yuan, H., Hansen, K. B., Zhang, J., Pierson, T. M., Markello, T. C., Fajardo, K. V. F., Holloman, C., Golas, G. A., Adams, D. R., Boerkoel, C. F., et al. (2014) · Nature Communications · doi:10.1038/ncomms4251 · Cited by 137 · see citing works
Retromer Mediates a Discrete Route of Local Membrane Delivery to Dendrites
Choy, R., Park, M., Temkin, P. A., Herring, B. E., Marley, A., Nicoll, R. A., & von Zastrow, M. (2014) · Neuron · doi:10.1016/j.neuron.2014.02.018 · Cited by 137 · cited 2× · see citing works
“…not been extensively addressed in NMDAR regulation, recent evidence points to a role of this protein complex in modulation of surface expression of these receptors (Wang, Zhao, & Zhang, 2013; Choy et al., 2014; Farias, Gershlick, & Bonifacino, 2014), by promoting receptor recycling to the membrane.”
BackgroundLeonard, A. S., Bayer, K. U., Merrill, M. A., Lim, I. A., Shea, M. A., Schulman, H., & Hell, J. W. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m205164200 · Cited by 136 · cited 1× · see citing works
“One of the major interacting partners for CaMKII is the GluN2B subunit of NMDARs (Bayer et al., 2001; Leonard, Lim, Hemsworth, Horne, & Hell, 1999; Leonard et al., 2002; Strack & Colbran, 1998).”
BackgroundYin, X., Takei, Y., Kido, M. A., & Hirokawa, N. (2011) · Neuron · doi:10.1016/j.neuron.2011.02.049 · Cited by 136 · see citing works
de Armentia, M. L., & Sah, P. (2003) · Journal of Neuroscience · doi:10.1523/jneurosci.23-17-06876.2003 · Cited by 134 · cited 1× · see citing works
“However, GluN2 subunits other than GluN2A can also mediate synaptic NMDAR currents in specific brain regions, such as in the amygdala, striatum and substantia nigra pars compacta (Lopez de Armentia & Sah, 2003; Brothwell et al., 2008; Logan, Partridge, Matta, Buonanno, & Vicini, 2007).”
BackgroundSupramodular structure and synergistic target binding of the N-terminal tandem PDZ domains of PSD-95
Long, J., Tochio, H., Wang, P., Fan, J., Sala, C., Niethammer, M., Sheng, M., & Zhang, M. (2003) · Journal of Molecular Biology · doi:10.1016/s0022-2836(03)00113-x · Cited by 134 · cited 1× · see citing works
“These MAGUKs are defined by the presence of three conserved PDZ domains, one SH3 domain followed by a catalytically inactive GK modular domain (Long et al., 2003; McGee et al., 2001; Doyle et al., 1996).”
BackgroundMechanisms and Function of Dendritic Exocytosis
Kennedy, M. J., & Ehlers, M. D. (2011) · Neuron · doi:10.1016/j.neuron.2011.02.032 · Cited by 132 · cited 1× · see citing works
“Dendritic exocytosis of many neurotransmitter receptors, including NMDARs, is a tightly regulated process (Kennedy & Ehlers, 2011).”
BackgroundMok, H., Shin, H., Kim, S., Lee, J.-R., Yoon, J., & Kim, E. (2002) · Journal of Neuroscience · doi:10.1523/jneurosci.22-13-05253.2002 · Cited by 132 · cited 2× · see citing works
“Indeed, KIF1B has been reported to interact directly with SAP97 and SAP102; however, its role in regulating the transport of NMDARs in the secretory pathway has not been determined (Mok et al., 2002).”
BackgroundSurface dynamics of GluN2B‐NMDA receptors controls plasticity of maturing glutamate synapses
Dupuis, J. P., Ladépêche, L., Seth, H., Bard, L., Varela, J. A., Mikasová, L., Bouchet, D., Rogemond, V., Honnorat, J., Hanse, E., et al. (2014) · The EMBO Journal · doi:10.1002/embj.201386356 · Cited by 132 · cited 3× · see citing works
“Interestingly, activated CaMKII recruits CKII and GluN2B to form a tripartite complex, which is required to maintain the phosphorylation of GluN2B at Ser-1480 by CKII (Sanz-Clemente, Gray, Ogilvie, Nicoll, & Roche, 2013).”
BackgroundmPins modulates PSD-95 and SAP102 trafficking and influences NMDA receptor surface expression
Sans, N., Wang, P. Y., Du, Q., Petralia, R., Wang, Y.-X., Nakka, S., Blumer, J., Macara, I., & Wenthold, R. (2005) · Nature Cell Biology · doi:10.1038/ncb1325 · Cited by 131 · cited 17× · see citing works
“SAP97 phosphorylation at Ser-39 drives the translocation of SAP97 from the ER to the post-synaptic compartment, whereas its phosphorylation at Ser-232 disrupts SAP97 interaction with GluN2A.”
BackgroundInfluentialKellermayer, B., Ferreira, J. S., Dupuis, J. P., Levet, F., Grillo‐Bosch, D., Bard, L., Linarès-Loyez, J., Bouchet, D., Choquet, D., Rusakov, D. A., et al. (2018) · Neuron · doi:10.1016/j.neuron.2018.09.012 · Cited by 125 · cited 4× · see citing works
“These two subtypes of NMDARs display substantial differences in their nanoscale organization, which changes during development in hippocampal neurons (Kellermayer et al., 2018).”
BackgroundInfluentialOgden, K. K., Chen, W., Swanger, S. A., McDaniel, M. J., Fan, L. Z., Hu, C., Tankovic, A., Kusumoto, H., Kosobucki, G. J., Schulien, A. J., et al. (2017) · PLoS Genetics · doi:10.1371/journal.pgen.1006536 · Cited by 124 · see citing works
Endocytosis and Degradative Sorting of NMDA Receptors by Conserved Membrane-Proximal Signals
Scott, D. B., Michailidis, I. E., Mu, Y., Logothetis, D. E., & Ehlers, M. (2004) · Journal of Neuroscience · doi:10.1523/jneurosci.0780-04.2004 · Cited by 123 · cited 2× · see citing works
“Although both subunits are initially present in early endosomes, the majority of GluN2A is sorted into late endosomes, as demonstrated by increased co-localization with the late endosomal marker Rab-9, whereas GluN2B is sorted into recycling endosomes, where it co-localizes with Rab-11 (Lavezzari et al., 2004; Scott e…”
BackgroundSNAP-25 is a target of protein kinase C phosphorylation critical to NMDA receptor trafficking
Lau, C. G., Takayasu, Y., Rodenas-Ruano, A., Paternain, A. V., Lerma, J., Bennett, M. V. L., & Zukin, R. S. (2010) · The Journal of Neuroscience · doi:10.1523/jneurosci.4933-08.2010 · Cited by 120 · cited 1× · see citing works
“Subsequently, SNAP25 was found to be a substrate of PKC and mutation of a single-SNAP25 phosphorylation site (Ser-187) could abolish PKC-induced insertion of NMDARs (Lau et al., 2010).”
BackgroundInternalization at glutamatergic synapses during development
Petralia, R. S., Wang, Y., & Wenthold, R. J. (2003) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2003.03074.x · Cited by 120 · see citing works
The role of SAP97 in synaptic glutamate receptor dynamics
Howard, M. A., Elias, G. M., Elias, L. A. B., Swat, W., & Nicoll, R. A. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0914422107 · Cited by 119 · cited 1× · see citing works
“Indeed, over-expression of either SAP97 or SAP102 fully restores glutamatergic transmission in neurons derived from PSD-93/PSD-95 double-knockout mice (Elias et al., 2006; Howard et al., 2010).”
BackgroundSupramolecular organization of NMDA receptors and the postsynaptic density
Frank, R., & Grant, S. G. N. (2017) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2017.05.019 · Cited by 119 · cited 1× · see citing works
“…binary interactions between individual GluN2 subunits with MAGUKs in vitro relies on these C-terminal PDZ-binding motifs, a recent study has revealed that they are dispensable for the formation of the 1.5 mega-Dalton NMDAR-MAGUK supercomplexes in vivo (Frank et al., 2016; Frank & Grant, 2017).”
BackgroundInfluentialCaMKII-dependent Phosphorylation Regulates SAP97/NR2A Interaction*
Gardoni, F., Mauceri, D., Fiorentini, C., Bellone, C., Missale, C., Cattabeni, F., & di Luca, M. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m303576200 · Cited by 118 · cited 1× · see citing works
“The function of SAP97 is tightly regulated by the phosphorylation of CaMKII on two key sites, Ser-39 (within the L27 domain) and Ser-232 (within the PDZ1 domain) (Gardoni et al., 2003; Mauceri, Gardoni, Marcello, & Luca, 2007).”
BackgroundPerszyk, R. E., DiRaddo, J. O., Strong, K. L., Low, C.-M., Ogden, K. K., Khatri, A., Vargish, G. A., Pelkey, K. A., Tricoire, L., Liotta, D. C., et al. (2016) · Molecular Pharmacology · doi:10.1124/mol.116.105130 · Cited by 116 · see citing works
Braithwaite, S., Adkisson, M., Leung, J., Nava, A., Masterson, B., Urfer, R., Oksenberg, D., & Nikolich, K. (2006) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2006.04837.x · Cited by 116 · cited 1× · see citing works
“…YEKL motif can be decreased by the striatal-enriched protein tyrosine phosphatase (STEP), which directly interacts with NMDAR subunits and PSD-95 and whose down-regulation leads to enhanced levels of GluN1, GluN2A and GluN2B subunits (Braithwaite et al., 2006; Won, Incontro, Nicoll, & Roche, 2016).”
BackgroundPSD-95 stabilizes NMDA receptors by inducing the degradation of STEP 61
Won, S., Incontro, S., Nicoll, R. A., & Roche, K. W. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1609702113 · Cited by 116 · cited 1× · see citing works
“More recently, PSD-95 has been shown to interact with the tyrosine phosphatase STEP-61 and promotes its degradation via the ubiquitin–proteasome system (Won et al., 2016).”
BackgroundSelf-citationActivation of Metabotropic Glutamate Receptor 1 Accelerates NMDA Receptor Trafficking
Lan, J.-Y., Skeberdis, V. A., Jover, T., Zheng, X., Bennett, M. V. L., & Zukin, R. S. (2001) · Journal of Neuroscience · doi:10.1523/jneurosci.21-16-06058.2001 · Cited by 115 · see citing works
Activated CaMKII Couples GluN2B and Casein Kinase 2 to Control Synaptic NMDA Receptors
Sanz-Clemente, A., Gray, J. A., Ogilvie, K. A., Nicoll, R. A., & Roche, K. W. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.02.011 · Cited by 114 · see citing works
Self-citationSingle-molecule imaging of the functional crosstalk between surface NMDA and dopamine D1 receptors
Ladépêche, L., Dupuis, J. P., Bouchet, D., Doudnikoff, É., Yang, L., Campagne, Y., Bézard, E., Hosy, E., & Groc, L. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1310145110 · Cited by 113 · cited 2× · see citing works
“, 2009), secreted proteases (Lesept, Chevilley, & Jezequel, 2016), growth factors (De Rossi, Harde, & Dupuis, 2016), cell surface receptors (Ladepeche et al., 2013; Mikasova et al., 2012) and hormones (Potier et al.”
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Research works printed but not linked: 6
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Cited by
Sorted by citations
Structure, Function, and Pharmacology of Glutamate Receptor Ion Channels
Hansen, K. B., Wollmuth, L. P., Bowie, D., Furukawa, H., Menniti, F. S., Sobolevsky, A. I., Swanson, G. T., Swanger, S. A., Greger, I. H., Nakagawa, T., et al. (2021) · Pharmacological Reviews · doi:10.1124/pharmrev.120.000131 · Cited by 686 · see citing works
The Role of Glutamate Receptors in Epilepsy
Chen, T., Huang, T., Lai, M., & Huang, C. (2023) · Biomedicines · doi:10.3390/biomedicines11030783 · Cited by 176 · see citing works
NMDA receptor functions in health and disease: Old actor, new dimensions
Dupuis, J. P., Nicole, O., & Groc, L. (2023) · Neuron · doi:10.1016/j.neuron.2023.05.002 · Cited by 171 · see citing works
Therapeutic potential of N-methyl-D-aspartate receptor modulators in psychiatry
Hanson, J. E., Yuan, H., Perszyk, R. E., Banke, T. G., Xing, H., Tsai, M., Menniti, F. S., & Traynelis, S. F. (2023) · Neuropsychopharmacology · doi:10.1038/s41386-023-01614-3 · Cited by 116 · see citing works
“It was recently discovered that GluN2A is also phosphorylated by CaMKII, leading to altered protein interactions, decreased surface expression and reduced synaptic function [51, 52].”
BackgroundSchizophrenia Genomics: Convergence on Synaptic Development, Adult Synaptic Plasticity, or Both?
Hall, J., & Bray, N. J. (2021) · Biological Psychiatry · doi:10.1016/j.biopsych.2021.10.018 · Cited by 86 · see citing works
“Both the glutamatergic NMDA receptor complex and voltage-gated calcium channels, which are strongly implicated in genetic risk for schizophrenia (15), play a central role in synaptic plasticity by allowing entry of Ca(21) into postsynaptic dendrites (66,67).”
BackgroundRen, L., Liu, C., Çifcibaşı, K., Ballmann, M., Rammes, G., Reyes, C. M., Tokalov, S. V., Klingl, A., Grünert, J., Goyal, K., et al. (2025) · Cancer Cell · doi:10.1016/j.ccell.2025.09.003 · Cited by 78 · see citing works
Mechanisms of NMDA receptor regulation
Mony, L., & Paoletti, P. (2023) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2023.102815 · Cited by 71 · see citing works
GRIN2B-related neurodevelopmental disorder: current understanding of pathophysiological mechanisms
Sabo, S. L., Lahr, J. M., Offer, M., Weekes, A. L., & Sceniak, M. P. (2023) · Frontiers in Synaptic Neuroscience · doi:10.3389/fnsyn.2022.1090865 · Cited by 63 · see citing works
“…patterns, GluN2B has been hypothesized to play roles in a variety of neurodevelopmental processes, including neuronal differentiation, dendritogenesis, synaptogenesis, circuit formation/refinement, and synaptic plasticity (Figure 1; Ewald and Cline, 2008; Myers et al., 2019; Vieira et al., 2020).”
BackgroundInfluentialAraki, S., Osuka, K., Takata, T., Tsuchiya, Y., & Watanabe, Y. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21217997 · Cited by 61 · see citing works
“The differential roles of GluN2A- and GluN2B-containing NMDARs in neurons have been extensively reviewed [36].”
BackgroundYang, X., Gong, R., Qin, L., Bao, Y., Fu, Y., Gao, S., Yang, H., Ni, J. D., Yuan, T., & Lü, W. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.111217 · Cited by 62 · see citing works
A Review of Molecular Imaging of Glutamate Receptors
Kim, J., Marton, J., Ametamey, S. M., & Cumming, P. D. (2020) · Molecules · doi:10.3390/molecules25204749 · Cited by 60 · see citing works
Ladagu, A., Olopade, F., Adejare, A., & Olopade, J. (2023) · Pharmaceuticals · doi:10.3390/ph16111535 · Cited by 51 · see citing works
“Therefore, there is mounting evidence that the GluN2B subunit is an essential subunit that requires attention when considering dementias related to a vast majority of neurodegenerative diseases [125,126].”
BackgroundLloyd‐Evans, E., & Waller‐Evans, H. (2020) · Essays in Biochemistry · doi:10.1042/ebc20200043 · Cited by 71 · see citing works
Vieira, M. M., Nguyen, T., Wu, K., Badger, J. D., Collins, B. M., Anggono, V., Lü, W., & Roche, K. W. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.108104 · Cited by 53 · see citing works
“Mutations in the CTD, however, also have damaging potential, since they often have dramatic effects on receptor trafficking and stabilization at the membrane (Liu et al., 2017), and consequently, can have a profound impact on synaptic transmission and plasticity (reviewed by Vieira et al., 2020).”
BackgroundSelf-citationStudying Synaptic Connectivity and Strength with Optogenetics and Patch-Clamp Electrophysiology
Linders, L. E., Supiot, L. F., Du, W., D’Angelo, R., Adan, R. A. H., Riga, D., & Meye, F. J. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms231911612 · Cited by 61 · see citing works
“Moreover, NMDAR subtypes with distinct decay kinetics may impact on the measure, and for relatively fast decaying NMDAR subtypes this approach may not be feasible [44].”
BackgroundNMDA Receptors in Neurodevelopmental Disorders: Pathophysiology and Disease Models
Tumdam, R., Hussein, Y., Garin-Shkolnik, T., & Stern, S. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms252212366 · Cited by 39 · see citing works
“In contrast to the GluN1 subunit, GluN2 expression fluctuates dynamically during embryonic brain development, reflecting an intricate regulation of stage-specific, region-specific, and cell-specific expression patterns [57].”
Irving, A. J., & Harvey, J. (2021) · Progress in Lipid Research · doi:10.1016/j.plipres.2021.101098 · Cited by 44 · see citing works
Regulation of membrane NMDA receptors by dynamics and protein interactions
Petit‐Pedrol, M., & Groc, L. (2020) · The Journal of Cell Biology · doi:10.1083/jcb.202006101 · Cited by 47 · see citing works
“cycling of NMDARs between intracellular pool and the plasma membrane relies on protein interactions and phosphorylation processes that have been well characterized (Trepanier et al., 2012; Sanz-Clemente et al., 2013b; Horak et al., 2014; Vieira et al., 2020).”
BackgroundMarino, J., Wigdahl, B. L., & Nonnemacher, M. R. (2020) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2020.00168 · Cited by 43 · see citing works
Post‐translational palmitoylation of ionotropic glutamate receptors in excitatory synaptic functions
Hayashi, T. (2020) · British Journal of Pharmacology · doi:10.1111/bph.15050 · Cited by 39 · see citing works
Liu, W., Li, Y., Zhao, T., Gong, M., Wang, X., Zhang, Y., Xu, L., Li, W., Li, Y., & Jia, J. (2023) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2023.102534 · Cited by 43 · see citing works
De novo GRIN2A variants associated with epilepsy and autism and literature review
Mangano, G. D., Riva, A., Fontana, A., Salpietro, V., Mangano, G. R., Nobile, G., Orsini, A. A., Iacomino, M., Battini, R., Astrea, G., et al. (2022) · Epilepsy & Behavior · doi:10.1016/j.yebeh.2022.108604 · Cited by 35 · see citing works
Puerarin Alleviates Vascular Cognitive Impairment in Vascular Dementia Rats
Zhu, T., Zhu, M., Qiu, Y., Wu, Z., Huang, N., Wan, G., Xu, J., Song, P., Wang, S., YaLing, Y., et al. (2021) · Frontiers in Behavioral Neuroscience · doi:10.3389/fnbeh.2021.717008 · Cited by 28 · see citing works
“, 2007; Xu and Zheng, 2007), which is associated with TRPM2 (Belrose and Jackson, 2018) and the NMDA subfamily of glutamate receptors (NMDAR) (Vieira et al., 2020).”
BackgroundYong, X. L., Zhang, L.-R., Yang, L., Chen, X.-M., Yu, X., Chandra, M., Livingstone, E., Tan, J. A., Widagdo, J., Vieira, M., et al. (2021) · bioRxiv · doi:10.1101/2021.01.11.425709 · Cited by 30
Self-citationDistinct regulation of tonic GABAergic inhibition by NMDA receptor subtypes
Wu, K., Castellano, D., Tian, Q., & Lü, W. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109960 · Cited by 33 · see citing works
“Importantly, GluN2A- and GluN2B-NMDARs exhibit differences in kinetics, ligand sensitivity, ion permeability, and interactions with intracellular proteins (Vieira et al., 2020).”
BackgroundRafe, M. R., Saha, P., & Bello, S. T. (2024) · Behavioural Brain Research · doi:10.1016/j.bbr.2024.115173 · Cited by 29 · see citing works
González‐Cota, A. L., Martínez-Flores, D., Rosendo‐Pineda, M. J., & Vaca, L. A. (2024) · Cell Calcium · doi:10.1016/j.ceca.2024.102856 · Cited by 38 · see citing works
Targeting NMDA Receptors in Emotional Disorders: Their Role in Neuroprotection
Wang, S., Bian, L.-H., Yin, Y., & Guo, J. (2022) · Brain Sciences · doi:10.3390/brainsci12101329 · Cited by 31 · see citing works
“GluN2C is expressed in the cerebellum and olfactory bulb two weeks after birth [24,25].”
BackgroundThe diverse and complex modes of action of anti-NMDA receptor autoantibodies
Wollmuth, L. P., Chan, K., & Groc, L. (2021) · Neuropharmacology · doi:10.1016/j.neuropharm.2021.108624 · Cited by 37 · see citing works
Herbrechter, R., Hube, N., Buchholz, R., & Reiner, A. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-021-03865-z · Cited by 38 · see citing works
“Within the NMDA receptor subfamily [17, 122], alternative splicing has been foremost reported for the GluN1 subunit.”
BackgroundAMPA and NMDA Receptor Trafficking at Cocaine-Generated Synapses
Wang, Y. Q., Huang, Y. H., Balakrishnan, S., Liu, L., Wang, Y. T., Nestler, E. J., Schlüter, O. M., & Dong, Y. (2021) · Journal of Neuroscience · doi:10.1523/jneurosci.1918-20.2021 · Cited by 30 · see citing works
“Role of CaMKII signaling in GluN2B NMDAR removal In many brain regions, the GluN2B-to-GluN2A switch of synaptic NMDARs marks the maturation of glutamatergic synapses during postnatal development (Carroll and Zukin, 2002; CullCandy and Leszkiewicz, 2004; Vieira et al., 2020).”
BackgroundБачурин, С. О., Махаева, Г. Ф., Shevtsova, E. F., Aksinenko, A. Y., Grigoriev, V. V., Shevtsov, P. N., Горева, Т. В., Епишина, Т. А., Ковалева, Н. В., Pushkareva, E. A., et al. (2021) · Molecules · doi:10.3390/molecules26185527 · Cited by 28 · see citing works
Grochowska, K. M., Sperveslage, M., Raman, R., Failla, A. V., Głów, D., Schulze, C., Laprell, L., Fehse, B., & Kreutz, M. R. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.112998 · Cited by 27 · see citing works
Kolcheva, M., Kortus, S., Krausová, B., Barackova, P., Misiachna, A., Danačíková, Š., Kaniakova, M., Hemelikova, K., Hotovec, M., Řeháková, K., et al. (2021) · Neuropharmacology · doi:10.1016/j.neuropharm.2021.108528 · Cited by 23 · see citing works
Luca, P. D., Mele, M., Tanqueiro, S. R., Napoli, F., Butkevičiūtė, U., Souto, A. C., Costa, R. O., Schwarz, A. P., Drexel, M., Sebastião, A. M., et al. (2025) · Journal of Biomedical Science · doi:10.1186/s12929-025-01164-4 · Cited by 25 · see citing works
“The GluN2B-containing NMDAR are characterized by an enhanced Ca 2 + -permeability and charge transfer, as well as by a slower rate of deactivation, rise and decay times when compared with the receptors with GluN2A subunits [62].”
Regulation of Synaptic NMDA Receptor Activity by Post-Translational Modifications
Tahiri, E., Corti, E., & Duarte, C. B. (2025) · Neurochemical Research · doi:10.1007/s11064-025-04346-6 · Cited by 21 · see citing works
“…synthesis and assembly of new receptors, which take place in the Golgi apparatus at the soma or in dendritic Golgi out - posts, their dendritic transport, the rate of receptor delivery to the plasma membrane, their lateral diffusion, and the inter - nalization, recycling and degradation [ 15–17].”
Xie, D., Zhang, P., You, S., Shen, Y., Xu, W., Zhan, C., & Zhang, J.-G. (2024) · Phytomedicine · doi:10.1016/j.phymed.2024.155583 · Cited by 21 · see citing works
Molecular Mechanisms Underlying NMDARs Dysfunction and Their Role in ADHD Pathogenesis
Kuś, J., Saramowicz, K., Czerniawska, M., Wiese, W., Siwecka, N., Rozpędek‐Kamińska, W., Kucharska-Lusina, A., Strzelecki, D., & Majsterek, I. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241612983 · Cited by 26 · see citing works
“Mutations were found in all domains (ATD, ABD, TM, and CTD), but most frequently in the ABD and TM regions [46].”
BackgroundInfluentialLiu, P., Wang, C., Chen, W., Kang, Y., Liu, W., Qiu, Z., Hayashi, T., Mizuno, K., Hattori, S., Fujisaki, H., et al. (2022) · Phytomedicine · doi:10.1016/j.phymed.2022.154594 · Cited by 23 · see citing works
Food for Thought: Leptin and Hippocampal Synaptic Function
Harvey, J. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.882158 · Cited by 20 · see citing works
SynapseJ: An Automated, Synapse Identification Macro for ImageJ
Manrique, J. F. M., Voit, P. R., Windsor, K. E., Karla, A. R., Rodriguez, S. R., & Beaudoin, G. M. J. (2021) · Frontiers in Neural Circuits · doi:10.3389/fncir.2021.731333 · Cited by 21 · see citing works
“Neurotransmitter receptors are localized at the postsynaptic membrane but may also be found on the plasma membrane away from the synapse and in intracellular vesicular stores (Bissen et al., 2019;Vieira et al., 2020).”
Meng, Y., & Shen, H.-L. (2022) · Journal of Pain Research · doi:10.2147/jpr.s367982 · Cited by 18 · see citing works
“GLuN1 and 3, GLuN2 consists of four subunits that play related roles in the central nervous system, and binds glutamate.(36) Through the c-terminal domain of the GluN2 subunit, NMDA connects to a huge signal transduction and scaffold protein network on the cytoplasmic side.”
BackgroundAltê, G. A., & Rodrigues, A. L. S. (2023) · Pharmaceuticals · doi:10.3390/ph16071013 · Cited by 19 · see citing works
“Regarding GluN2, four different subunits (GluN2A-D) are present throughout the central nervous system [22].”
BackgroundTwo gates mediate NMDA receptor activity and are under subunit-specific regulation
Amin, J. B., He, M., Prasad, R., Leng, X., Zhou, H., & Wollmuth, L. P. (2023) · Nature Communications · doi:10.1038/s41467-023-37260-y · Cited by 19 · see citing works
Nasyrova, R., Khasanova, A. K., Altynbekov, K. S., Asadullin, A., Markina, E. A., Gayduk, A., Shipulin, G., Petrova, M. M., & Shnayder, N. (2022) · Nutrients · doi:10.3390/nu14235142 · Cited by 16 · see citing works
“At the same time, NMDAR is formed by two GluN1 subunits and either two GluN2 subunits, or a combination of GluN2 and GluN3 subunits, which form a channel (pore) [29].”
BackgroundHuang, W., Wang, Z., Wang, G., Li, K., Jin, Y., & Zhao, F. (2022) · Environmental Pollution · doi:10.1016/j.envpol.2022.119813 · Cited by 17 · see citing works
Skrenkova, K., Song, J.-M., Kortus, S., Kolcheva, M., Netolicky, J., Hemelikova, K., Kaniakova, M., Krausová, B., Kučera, T., Korábečný, J., et al. (2020) · Scientific Reports · doi:10.1038/s41598-020-75646-w · Cited by 15 · see citing works
Influence of Gestational Chlorpyrifos Exposure on ASD-like Behaviors in an fmr1-KO Rat Model
Pérez-Fernández, C., Montoya, M. M., Morales-Navas, M., Guardia-Escoté, L., Cabré, M., Colomina, M., Giménez, E., & Sánchez-Santed, F. (2022) · Molecular Neurobiology · doi:10.1007/s12035-022-02933-0 · Cited by 14 · see citing works
Yates, J. R. (2024) · Progress in Neuro-Psychopharmacology and Biological Psychiatry · doi:10.1016/j.pnpbp.2024.111107 · Cited by 15 · see citing works
Ugale, D. V., Deshmukh, R., Lokwani, D. K., Reddy, P. N., Khadse, S., Chaudhari, P., & Kulkarni, P. (2023) · Molecular diversity · doi:10.1007/s11030-023-10656-0 · Cited by 13 · see citing works
“Thus, alteration in function of NMDAR is one of the mechanisms influencing the AD [30, 31].”
Yin, Y., Liu, Y., Zhu, M., Wang, H., Qiu, Y., Wan, G., & Li, P. (2022) · Physiology & Behavior · doi:10.1016/j.physbeh.2022.113777 · Cited by 15 · see citing works
Palmitoylation Controls NMDA Receptor Function and Steroid Sensitivity
Hubálková, P., Ladislav, M., Vyklický, V., Smejkalová, T., Krausová, B. H., Kysilov, B., Krůšek, J., Naimová, Ž., Kořı́nek, M., Chodounská, H., et al. (2021) · Journal of Neuroscience · doi:10.1523/jneurosci.2654-20.2021 · Cited by 18 · see citing works
“NMDAR phosphorylation by kinases, such as PKC or CaMKII, can influence receptor trafficking and channel gating, resulting in increased synaptic strength (Vieira et al., 2020).”
BackgroundWang, X.-N., Mei, D.-Q., Gou, L., Zhao, S., Gao, C., Guo, J., Luo, S.-Y., Guo, B., Yang, Z.-G., Wang, Q., et al. (2023) · Neuroscience · doi:10.1016/j.neuroscience.2023.06.018 · Cited by 12 · see citing works
Kang, J. S., Baek, J. H., Park, H., Rehman, N. U., Chung, H. J., Lee, D.-K., Oh, S., & Kim, H. J. (2026) · International Journal on Biological Sciences · doi:10.7150/ijbs.123740 · Cited by 11 · see citing works
“GluN2B can produce nitric oxide (NO) through its interaction with postsynaptic density protein 95 and neuronal nitric oxide synthase [47].”
Adapting the endoplasmic reticulum proteostasis rescues epilepsy-associated NMDA receptor variants
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Role of actin cytoskeleton in the organization and function of ionotropic glutamate receptors
Dutta, P., Bharti, P., Kumar, J., & Maiti, S. (2021) · Current Research in Structural Biology · doi:10.1016/j.crstbi.2021.10.001 · Cited by 11 · see citing works
“Studying the detailed molecular interaction of cytoskeletal proteins with iGluRs is required to understand synaptic plasticity (Traynelis et al., 2010; Van Spronsen and Hoogenraad, 2010; Vyas and Montgomery, 2016).”
BackgroundLiu, Y.-S., Tang, H., Zhang, J.-F., Li, D., & Kou, Z.-W. (2025) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2025.07.027 · Cited by 9 · see citing works
“This was followed by a sharp decline in GluN2B levels, which is consistent with the developmental switch to GluN2A-containing NMDARs [22].”
Upreti, S., Nag, T., & Ghosh, M. P. (2023) · Experimental Eye Research · doi:10.1016/j.exer.2023.109740 · Cited by 9
Hu, N., Hu, Z., Ondrejčák, T., Yu, P., Zhang, Y., Yang, Y., Klyubin, I. V., Kennelly, S., & Rowan, M. J. (2022) · Neural Regeneration Research · doi:10.4103/1673-5374.360166 · Cited by 11 · see citing works
“Extrasynaptic NMDAR have been considered important mediators of neurotoxicity, while synaptic NMDAR are mainly involved in normal cognitive function (Vieira et al., 2020).”
BackgroundWang, J., Yu, X.-F., Song, S., Zhang, Y., Cao, J., Jin, C.-F., Bao, Z.-M., Wang, B., & Hu, J.-J. (2025) · Fish and Shellfish Immunology · doi:10.1016/j.fsi.2025.110290 · Cited by 8 · see citing works
Serwach, K., Nurowska, E., Klukowska, M., Zabłocka, B., & Gruszczynska-Biegala, J. (2023) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-023-05028-8 · Cited by 8 · see citing works
“NMDAR proteins are synthesized in the ER and then directed to the Golgi apparatus [46].”
BackgroundChen, X., Zhu, H., liu, X., Li, Q., & Dong, M. (2023) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2023.117236 · Cited by 9 · see citing works
Ashourpour, F., Jafari, A., & Babaei, P. (2020) · International Journal of Neuroscience · doi:10.1080/00207454.2020.1837800 · Cited by 9 · see citing works
“LTP induction promotes the recruitment of AMPARs, growth of dendritic spines and longlasting increase in synaptic efficacy as well [19].”
BackgroundBiosca-Brull, J., Guardia-Escoté, L., Basaure, P., Cabré, M., Blanco, J., Pérez-Fernández, C., Sánchez-Santed, F., Domingo, J., & Colomina, M. (2023) · Environmental Research · doi:10.1016/j.envres.2023.115461 · Cited by 7 · see citing works
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Regulation of NMDA Receptor Signaling at Single Synapses by Human Anti-NMDA Receptor Antibodies
Dean, C. A., Metzbower, S. R., Dessain, S. K., Blanpied, T. A., & Benavides, D. R. (2022) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2022.940005 · Cited by 11 · see citing works
Postsynaptic signaling at glutamatergic synapses as therapeutic targets.
Ge, Y., & Wang, Y.-T. (2022) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2022.102585 · Cited by 7 · see citing works
Horak, M., Barackova, P., Langore, E., Netolicky, J., Rivas-Ramírez, P., & Řeháková, K. (2021) · Frontiers in Neuroscience · doi:10.3389/fnins.2021.603715 · Cited by 7 · see citing works
“N-methyl-D-aspartate receptors (NMDARs) are ionotropic glutamate receptors that play an essential role in mediating excitatory neurotransmission (Traynelis et al., 2010; Vieira et al., 2020).”
BackgroundMolecular Physiology of the Neuronal Synapse
Ramírez-Expósito, M. J., Cueto-Ureña, C., & Martínez-Martos, J. M. (2026) · Current Issues in Molecular Biology · doi:10.3390/cimb48010088 · Cited by 6 · see citing works
“NMDAR trafficking is a complex process involving biosynthesis, dendritic transport, exocytosis, lateral diffusion, endocytosis, recycling, and degradation, all tightly controlled by protein–protein interactions involving the cytoplasmic carboxyl termini (CTDs) of NMDAR subunits [48].”
InfluentialCognitive loss after brain trauma results from sex-specific activation of synaptic pruning processes
Arizanovska, D., Bush, G., Dallera, C. A., Folorunso, O. O., Frye, J. B., Doyle, K. P., Jagid, J. R., Wolosker, H., de Mônaco, B. A., Cordeiro, J. G., et al. (2025) · Brain · doi:10.1093/brain/awaf293 · Cited by 6 · see citing works
“30,49,51,52 While glutamate levels stabilize quickly after brain injury, we show prolonged increases in the NMDAR co-agonist D -serine.”
Yang, S.-Z., Shen, T., Yu, M.-H., Wu, T.-T., Qian, L.-H., Liu, W., Wang, T., & Huang, X.-H. (2025) · Communications Biology · doi:10.1038/s42003-025-08296-1 · Cited by 6 · see citing works
“Thesereceptorsplayacrucialroleinglutamatergictransmission, synapticplasticity,andneuraldevelopmentbyformingionchannels permeabletoNa + , K + , and Ca 2 + , thereby being vital for signaling and function 36,63 .”
GRIN2A and Schizophrenia: Scientific Evidence and Biological Mechanisms
Sheng, X.-M., & Guan, W. (2024) · Current Neuropharmacology · doi:10.2174/011570159x327712241023084944 · Cited by 7 · see citing works
“These differences determine the time course of NMDAR-mediated excitatory postsynaptic currents, which affect synaptic integration and plasticity in various brain regions [35].”
InfluentialMyosin Va-dependent Transport of NMDA Receptors in Hippocampal Neurons
Gong, R., Qin, L., Chen, L., Wang, N., Bao, Y., & Lu, W. (2024) · Neuroscience Bulletin · doi:10.1007/s12264-023-01174-y · Cited by 5 · see citing works
Zhang, Y., Yang, Y., Hu, Z., Zhu, M., Qin, S., Yu, P., Li, B., Xu, J., Ondrejčák, T., Klyubin, I. V., et al. (2022) · Journal of Alzheimer s Disease · doi:10.3233/jad-220351 · Cited by 8 · see citing works
“Numerous studies have shown that synaptic NMDARs are mainly involved in normal cognitive function, while extrasynaptic NMDARs are important mediators of neurotoxicity [60].”
BackgroundSALM4 negatively regulates NMDA receptor function and fear memory consolidation
Lie, E., Yeo, Y., Lee, E., Shin, W., Kim, K., Han, K. A., Yang, E., Choi, T.-Y., Bae, M. H., Lee, S., et al. (2021) · Communications Biology · doi:10.1038/s42003-021-02656-3 · Cited by 5 · see citing works
Bai, H.-H., Zhang, Q., Wu, S., Gao, Y., Li, J., Bai, X., Yang, X., Liu, X.-X., Dang, J.-N., Yang, X. Z., et al. (2025) · PLoS Biology · doi:10.1371/journal.pbio.3003516 · Cited by 3 · see citing works
“Given the lower mobility of GluN2A than GluN2B receptors at postsynaptic membranes [53–55], the nerve injury-induced switch might underpin the persistence of chronic pain.”
Kang, M., Kim, S., Shin, W., Kim, K., Jung, Y., Choi, W., Paik, S., & Kim, E. (2025) · Science Advances · doi:10.1126/sciadv.adr7691 · Cited by 4 · see citing works
“The GluN2B subunit of NMDARs is expressed early in development and regulates neuronal and synaptic development, function, and signaling ( 20 – 22 , 24 , 27 , 28 ).”
Imiruaye, O. E., Perez, I. G., Carson, B. C., Crouzet, C., Garcia, J., Han, D., & Bhattacharya, S. (2025) · Frontiers in Neuroscience · doi:10.3389/fnins.2025.1649625 · Cited by 4 · see citing works
Kellner, S., & Berlin, S. (2024) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-024-05243-x · Cited by 5 · see citing works
Development of network oscillations through adolescence in male and female rats
Sibilska, S., Mofleh, R., & Kocsis, B. (2023) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2023.1135154 · Cited by 4 · see citing works
“The two receptors have divergent roles in synaptic transmission, plasticity, and neurodevelopment [see rev. Hensch, 2004; Paoletti et al., 2013; Shipton and Paulsen, 2014; Baez et al., 2018; Franchini et al., 2020; Vieira et al., 2020].”
BackgroundPharmacological Potential of 3-Benzazepines in NMDAR-Linked Pathophysiological Processes
Ritter, N., Disse, P., Wünsch, B., Seebohm, G., & Strutz‐Seebohm, N. (2023) · Biomedicines · doi:10.3390/biomedicines11051367 · Cited by 4 · see citing works
“Since the different GluN2 subunits impart different properties to the GluN receptor, various diseases are attributed to the NMDAR due to dysfunctions of the GluN2 subunits [48].”
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Srivastava, J., Yadav, J., & Dubey, N. (2026) · Cognitive Neurodynamics · doi:10.1007/s11571-026-10446-y · Cited by 3 · see citing works
NMDA Receptors in Neuropathic Pain: From Mechanisms to Therapeutic Strategies
Li, X.-Y., Fang, Z.-M., Guo, S.-J., Jia, L.-N., Sun, T., Ma, J.-L., & Zheng, Y.-L. (2026) · The Neuroscientist · doi:10.1177/10738584251410528 · Cited by 3 · see citing works
“These receptors demonstrate prolonged activation kinetics and higher calcium permeability as compared with GluN2A counterparts, properties that facilitate sustained Ca² + influx required for LTP in spinal nociceptive synapses—a cellular correlate of central sensitization (Vieira et al 2020).”
Chen, Y., Xu, Y.-H., Zhang, J., Feng, C., Chen, J., Song, Y., Pan, J.-Y., Zhu, J., & Cheng, H. (2026) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2025.1720876 · Cited by 3 · see citing works
Le, G. H., & McIntyre, R. S. (2026) · Expert Opinion on Therapeutic Targets · doi:10.1080/14728222.2026.2619757 · Cited by 3 · see citing works
“Glutamate exhibits higher relative affinity for the NR2D (half maximal effective concentration (EC 50 ) ≈ 0.4 µM) relative to other subunits (NR2C, EC 50 ≈1 µM > NR2B, EC 50 ≈2 µM > NR2A, EC 50 ≈4 µM) [71].”
InfluentialZhang, X., Cai, W., Wang, C., & Tian, J. (2025) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2025.108888 · Cited by 5 · see citing works
Kim, H., Jeon, Y., Kim, S., Guo, Y., Kim, D., Jang, G., Brasch, J., Um, J., & Ko, J. (2025) · Progress in neurobiology · doi:10.1016/j.pneurobio.2025.102772 · Cited by 3 · see citing works
Nelonemdaz Treatment for Patients With Out-of-Hospital Cardiac Arrest: A Randomized Clinical Trial
Chun, B. J., Yeom, S. R., Chung, S. P., Lee, Y. H., Lee, J., Kim, Y.-H., Lee, J.-S., Lee, J.-S., An, C., Gwag, B.-J., et al. (2025) · Critical Care Medicine · doi:10.1097/ccm.0000000000006579 · Cited by 3
Drug Repurposing and Screening for Multiple Sclerosis Targeting Microglia and Macrophages
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“Although predominantly expressed in neurons, NMDARs are also present in astrocytes [27, 28] and activated microglia [29].”
Nayan, N. M., Kadir, S. S. A., Husin, A., & Siran, R. (2024) · Physiology and Behavior · doi:10.1016/j.physbeh.2024.114546 · Cited by 3 · see citing works
Urrego-Morales, O., Gil-Lievana, E., Ramírez-Mejía, G., Rodríguez-Durán, L. F., Escobar, M. L., Delint-Ramírez, I., & Bermúdez-Rattoni, F. (2023) · Neurobiology of Learning and Memory · doi:10.1016/j.nlm.2023.107733 · Cited by 3 · see citing works
Gale, J., Kosobucki, G. J., Hartnett-Scott, K. A., & Aizenman, E. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.773455 · Cited by 3 · see citing works
“The GluN2 subtype dictates many of the NMDAR’s characteristics such as its biophysical, pharmacological, and signaling properties, as well as its spatiotemporal pattern of expression (Monyer et al., 1992; Watanabe et al., 1994; Paoletti et al., 2013; Vieira et al., 2020).”
BackgroundA GluN2B disease-associated variant promotes the degradation of NMDA receptors via autophagy
Benske, T. M., Williams, M. P., Zhang, P.-P., Palumbo, A. J., & Mu, T.-W. (2026) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2026.111147 · Cited by 2 · see citing works
Prenatal maternal HFD exposure impairs cognition via a hippocampal NMDA mechanism
Chen, K.-R., Ho, Y.-C., Huang, C.-W., Yu, L., & Kuo, P.-L. (2025) · Translational Psychiatry · doi:10.1038/s41398-025-03520-2 · Cited by 2 · see citing works
“Quantitative analysis of fEPSP evolution at the indicated group (Right).”
Chapman, C. A., Povysheva, N. V., Johnson, J. W., & Jacob, T. C. (2025) · Neuropharmacology · doi:10.1016/j.neuropharm.2025.110624 · Cited by 1 · see citing works
“GluN2A and GluN2B are the most prevalent GluN2 sub-units, and they convey higher open channel probability, calcium permeability, and Mg 2 + sensitivity when assembled into di-or tri-heteromeric receptors than do the GluN2C and GluN2D subunits (Glasgow et al., 2015; Vieira et al., 2020).”
Netolicky, J., Zahumenská, P., Misiachna, A., Kolcheva, M., Řeháková, K., Hemelikova, K., Kortus, S., Langore, E., Doderović, J., Ladislav, M., et al. (2025) · Journal of Neuroscience · doi:10.1523/jneurosci.0226-24.2025 · Cited by 2 · see citing works
“Eight known splice variants of the GluN1 subunit arise from a single gene, and there are four di ff erent genes for the GluN2 subunits: GluN2A, GluN2B, GluN2C, and GluN2D (Sanz-Clemente et al., 2012; Vieira et al., 2020; Hansen et al., 2021).”
- Authors
- Vieira, M., Yong, X. L. H., Roche, K. W., & Anggono, V.
- Affiliations
- National Institutes of Health (US)
- The University of Queensland (AU)
- Corresponding author
- Roche, Katherine W.
- Anggono, Victor
- Venue
- Journal of Neurochemistry
- Publisher
- Wiley
- Published
- 2020-02-16
- Volume
- 154
- Issue
- 2
- Pages
- 121-143
- ISSN
- 0022-3042 (ISSN-L)
- 1471-4159
- PMC
- PMC7351600
- OpenAlex
- W3001459179
- Cited by
- 151
- References
- 298
- Citations by year
- 2026: 17 · 2025: 31 · 2024: 19 · 2023: 30 · 2022: 22 · 2021: 23 · 2020: 9
- FWCI
- 2.91
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- Locations
- Journal of Neurochemistry (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- Australian Research Council (DP190101390)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Amino Acid Enzymes and Metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
- Keywords
- NMDA receptor, GluN2 subunits, GluN1 subunit, receptor trafficking, synaptic plasticity, ion channel properties, synaptic proteins, receptor internalization
- MeSH terms
- Animals, Humans, Receptors, N-Methyl-D-Aspartate, Protein Subunits, Protein Transport, Dendritic Spines
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