Regulation of AMPA receptor surface diffusion by PSD-95 slots

Opazo, Patricio; Sainlos, Matthieu; Choquet, Daniel

doi:10.1016/j.conb.2011.10.010

Cited by 234Neuroscience and Neuropharmacology ResearchNicotinic Acetylcholine Receptors StudyGenetics and Neurodevelopmental Disorders

Regulation of AMPA receptor surface diffusion by PSD-95 slots

Opazo, Patricio, Sainlos, Matthieu, Choquet, Daniel·2012·Current Opinion in Neurobiology

DOI 10.1016/j.conb.2011.10.010

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Abstract

Excitatory synaptic transmission is largely mediated by AMPA receptors (AMPARs) present at the postsynaptic density. Recent studies in single molecule tracking of AMPAR has revealed that extrasynaptic AMPARs are highly mobile and thus might serve as a readily available pool for their synaptic recruitment during synaptic plasticity events such as long-term potentiation (LTP). Because this hypothesis relies on the cell's ability to increase the number of diffusional traps or 'slots' at synapses during LTP, we will review a number of protein-protein interactions that might impact AMPARs lateral diffusion and thus potentially serve as slots. Recent studies have identified the interaction between the AMPAR-Stargazin complex and PSD-95 as the minimal components of the diffusional trapping slot. We will overview the molecular basis of this critical interaction, its activity-dependent regulation and its potential contribution to LTP.

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Delivery of AMPARs to synapses requires binding of TARPs via their PDZ binding motifs to PSD-95.
“It is now well established that the delivery of AMPARs to synapses requires the binding of TARPs, via their PDZ binding motifs (PBMs), to PSD-95 (278, 279, 286, 289, 294).”
From Synaptic memory and CaMKII (2023) · cites this paper as [286]
AMPARs are highly dynamic, undergoing continuous endocytosis, exocytosis, lateral diffusion, reversible trapping at PSD, and modifications in channel properties.
“AMPARs are highly dynamic, undergoing continuous endocytosis, exocytosis, lateral diffusion in the plane of the membrane, reversible trapping at synapses at the post-synaptic density (PSD), and modifications in channel properties (Opazo et al., 2012, Huganir and Nicoll, 2013, Malinow and Malenka, 2002).”
From The AMPA Receptor Code of Synaptic Plasticity (2018) · cites this paper as Opazo et al., 2012
Phosphorylation of the TARP C-terminus reduces interaction with membrane lipids and facilitates interaction with PSD95, serving to trap the TARP/AMPAR complex with the PSD.
“Phosphorylation reduces the interaction with membrane lipids and facilitates interaction with PSD95, serving to trap the TARP/AMPAR complex with the PSD (Opazo et al., 2012, Bats et al., 2007, Sheng et al., 2018).”
From The AMPA Receptor Code of Synaptic Plasticity (2018) · cites this paper as Opazo et al., 2012
The post-synaptic density contains 'slots' that might be occupied by AMPARs supplied by lateral diffusion from the peri-synaptic region.
“A prominent model of synaptic strength posits that the post-synaptic density (PSD), a dense network of synaptic scaffolding, adhesion and cytoskeletal proteins, contains ‘slots’ that might be occupied by AMPARs supplied by lateral diffusion from the peri-synaptic region (Opazo et al., 2012, Huganir and Nicoll, 2013, Kessels and Malinow, 2009).”
From The AMPA Receptor Code of Synaptic Plasticity (2018) · cites this paper as Opazo et al., 2012
In the plane of the plasma membrane, AMPARs are highly mobile but become trapped in PSD slots.
“In the plane of the plasma membrane, AMPARs are highly mobile but become trapped in PSD slots (Opazo et al., 2012).”
From The AMPA Receptor Code of Synaptic Plasticity (2018) · cites this paper as Opazo et al., 2012

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Dakoji, S., Tomita, S., Karimzadegan, S., Nicoll, R. A., & Bredt, D. S. (2003) · Neuropharmacology · doi:10.1016/s0028-3908(03)00267-3 · Cited by 104 · see citing works
Synaptic SAP97 Isoforms Regulate AMPA Receptor Dynamics and Access to Presynaptic Glutamate
Waites, C. L., Specht, C. G., Härtel, K., Leal-Ortiz, S., Genoux, D., Li, D., Drisdel, R. C., Jeyifous, O., Cheyne, J. E., Green, W. N., et al. (2009) · The Journal of Neuroscience · doi:10.1523/jneurosci.4431-08.2009 · Cited by 97 · see citing works
Roles of stargazin and phosphorylation in the control of AMPA receptor subcellular distribution
Kessels, H. W. H. G., Kopec, C. D., Klein, M. E., & Malinow, R. (2009) · Nature Neuroscience · doi:10.1038/nn.2340 · Cited by 96 · see citing works
Interaction of NE-dlg/SAP102, a Neuronal and Endocrine Tissue-specific Membrane-associated Guanylate Kinase Protein, with Calmodulin and PSD-95/SAP90
Masuko, N., Makino, K., Kuwahara, H., Fukunaga, K., Sudo, T., Araki, N., Yamamoto, H., Yamada, Y., Miyamoto, E., & Saya, H. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.9.5782 · Cited by 89 · see citing works
Requirement of N-terminal Cysteines of PSD-95 for PSD-95 Multimerization and Ternary Complex Formation, but Not for Binding to Potassium Channel Kv1.4
Hsueh, Y., & Sheng, M. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.1.532 · Cited by 86 · see citing works
Stargazin and Other Transmembrane AMPA Receptor Regulating Proteins Interact with Synaptic Scaffolding Protein MAGI-2 in Brain
Deng, F., Price, M. G., Davis, C., Mori, M., & Burgess, D. L. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.1851-06.2006 · Cited by 82 · see citing works
Trafficking of AMPA Receptors at Plasma Membranes of Hippocampal Neurons
Tao-Cheng, J.-H., Crocker, V. T., Winters, C. A., Azzam, R., Chludzinski, J., & Reese, T. S. (2011) · The Journal of Neuroscience · doi:10.1523/jneurosci.4745-10.2011 · Cited by 82 · see citing works
Assembly and Stoichiometry of the AMPA Receptor and Transmembrane AMPA Receptor Regulatory Protein Complex
Kim, K. S., Yan, D., & Tomita, S. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.3909-09.2010 · Cited by 80 · see citing works
Lipid- and protein-mediated multimerization of PSD-95: implications for receptor clustering and assembly of synaptic protein networks
Christopherson, K. S., Sweeney, N. T., Craven, S. E., Kang, R., El-Husseini, A., & Bredt, D. S. (2003) · Journal of Cell Science · doi:10.1242/jcs.00617 · Cited by 70 · see citing works
Different Domains of the AMPA Receptor Direct Stargazin-mediated Trafficking and Stargazin-mediated Modulation of Kinetics
Bedoukian, M. A., Weeks, A. M., & Partin, K. M. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m600679200 · Cited by 68 · see citing works
Dynamin-dependent Membrane Drift Recruits AMPA Receptors to Dendritic Spines
Jaskolski, F., Mayo-Martin, M. B., Jane, D. E., & Henley, J. M. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m808401200 · Cited by 65 · see citing works
Synaptic Clustering of PSD-95 Is Regulated by c-Abl through Tyrosine Phosphorylation
de Arce, K. P., Varela‐Nallar, L., Farias, O., Cifuentes, A., Bull, P., Couch, B. A., Koleske, A. J., Inestrosa, N. C., & Alvarez, A. R. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.2024-09.2010 · Cited by 59 · see citing works
Interaction between SAP97 and PSD-95, Two Maguk Proteins Involved in Synaptic Trafficking of AMPA Receptors
Cai, C., Li, H., Rivera, C., & KEINÄNEN, K. P. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m505886200 · Cited by 50 · see citing works
Creating Conformational Entropy by Increasing Interdomain Mobility in Ligand Binding Regulation: A Revisit to N-Terminal Tandem PDZ Domains of PSD-95
Wang, W., Weng, J., Zhang, X., Liu, M., & Zhang, M. (2008) · Journal of the American Chemical Society · doi:10.1021/ja8076022 · Cited by 50 · see citing works
Domain Orientation in the N-Terminal PDZ Tandem from PSD-95 Is Maintained in the Full-Length Protein
McCann, J. J., Zheng, L., Chiantia, S., & Bowen, M. E. (2011) · Structure · doi:10.1016/j.str.2011.02.017 · Cited by 41 · see citing works
Bidirectional redistribution of AMPA but not NMDA receptors after perforant path simulation in the adult rat hippocampus in vivo
Moga, D. E., Shapiro, M. L., & Morrison, J. H. (2006) · Hippocampus · doi:10.1002/hipo.20227 · Cited by 22 · see citing works
Self-directed assembly and clustering of the cytoplasmic domains of inwardly rectifying Kir2.1 potassium channels on association with PSD-95
Fomina, S. A., Howard, T. D., Sleator, O. K., Golovanova, M., O’Ryan, L., Leyland, M. L., Grossmann, J. G., Collins, R. F., & Prince, S. M. (2011) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2011.06.021 · Cited by 17 · see citing works
NMR Studies of Interactions between C-Terminal Tail of Kir2.1 Channel and PDZ1,2 Domains of PSD95
Pegan, S. D., Tan, J. T., Huang, A., Slesinger, P. A., Riek, R., & Choe, S. (2007) · Biochemistry · doi:10.1021/bi062228q · Cited by 17 · see citing works
Subunit-specific surface mobility of differentially labeled AMPA receptor subunits
Kropf, M., Rey, G., Glauser, L., Kulangara, K., Johnsson, K., & Hirling, H. (2008) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2008.02.014 · Cited by 15 · see citing works
Two modes of interaction between the membrane-embedded TARP stargazin’s C-terminal domain and the bilayer visualized by electron crystallography
Roberts, M. F., Taylor, D. W., & Unger, V. M. (2011) · Journal of Structural Biology · doi:10.1016/j.jsb.2011.03.012 · Cited by 6 · see citing works
Proteins involved in the synaptic organization of AMPA (α-amino-3-hydroxy-5-methylisoxazolepropionate) receptors
Henley, J. M. (2001) · Biochemical Society Transactions · doi:10.1042/bst0290485 · Cited by 4 · see citing works

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AMPARs and Synaptic Plasticity: The Last 25 Years
Huganir, R. L., & Nicoll, R. A. (2013) · Neuron · doi:10.1016/j.neuron.2013.10.025 · Cited by 968 · see citing works
The AMPA Receptor Code of Synaptic Plasticity
Diering, G. H., & Huganir, R. L. (2018) · Neuron · doi:10.1016/j.neuron.2018.10.018 · Cited by 844 · see citing works
A Brief History of Long-Term Potentiation
Nicoll, R. A. (2017) · Neuron · doi:10.1016/j.neuron.2016.12.015 · Cited by 841 · see citing works
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
Super-Resolution Imaging Reveals That AMPA Receptors Inside Synapses Are Dynamically Organized in Nanodomains Regulated by PSD95
Nair, D., Hosy, E., Petersen, J. D., Constals, A., Giannone, G., Choquet, D., & Sibarita, J.-B. (2013) · Journal of Neuroscience · doi:10.1523/jneurosci.2381-12.2013 · Cited by 617 · see citing works
Self-citation
The Dynamic Synapse
Choquet, D., & Triller, A. (2013) · Neuron · doi:10.1016/j.neuron.2013.10.013 · Cited by 515 · see citing works
Self-citation
Synaptic AMPA receptor composition in development, plasticity and disease
Henley, J. M., & Wilkinson, K. A. (2016) · Nature reviews. Neuroscience · doi:10.1038/nrn.2016.37 · Cited by 506 · see citing works
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 · see citing works
Balance and Stability of Synaptic Structures during Synaptic Plasticity
Meyer, D., Bonhoeffer, T., & Scheuss, V. (2014) · Neuron · doi:10.1016/j.neuron.2014.02.031 · Cited by 395 · see citing works
Transcellular Nanoalignment of Synaptic Function
Biederer, T., Kaeser, P. S., & Blanpied, T. A. (2017) · Neuron · doi:10.1016/j.neuron.2017.10.006 · Cited by 352 · see citing works
BDNF mechanisms in late LTP formation: A synthesis and breakdown
Panja, D., & Bramham, C. R. (2014) · Neuropharmacology · doi:10.1016/j.neuropharm.2013.06.024 · Cited by 336 · see citing works
Tracking single molecules at work in living cells
Kusumi, A., Tsunoyama, T. A., Hirosawa, K. M., Kasai, R. S., & Fujiwara, T. K. (2014) · Nature Chemical Biology · doi:10.1038/nchembio.1558 · Cited by 333 · see citing works
Multiple Autism-Linked Genes Mediate Synapse Elimination via Proteasomal Degradation of a Synaptic Scaffold PSD-95
Tsai, N.-P., Wilkerson, J. R., Guo, W., Maksimova, M. A., DeMartino, G. N., Cowan, C. W., & Huber, K. M. (2012) · Cell · doi:10.1016/j.cell.2012.11.040 · Cited by 316 · see citing works
Metabolic Turnover of Synaptic Proteins: Kinetics, Interdependencies and Implications for Synaptic Maintenance
Cohen, L. D., Zuchman, R., Sorokina, O., Müller, A., Dieterich, D. C., Armstrong, J. D., Ziv, T., & Ziv, N. E. (2013) · PLoS ONE · doi:10.1371/journal.pone.0063191 · Cited by 215 · see citing works
The autism and schizophrenia associated gene CYFIP1 is critical for the maintenance of dendritic complexity and the stabilization of mature spines
Pathania, M., Davenport, E. C., Muir, J., Sheehan, D. F., López-Doménech, G., & Kittler, J. T. (2014) · Translational Psychiatry · doi:10.1038/tp.2014.16 · Cited by 189 · see citing works
AMPA-silent synapses in brain development and pathology
Hanse, E., Seth, H., & Riebe, I. (2013) · Nature reviews. Neuroscience · doi:10.1038/nrn3642 · Cited by 175 · see citing works
Phase Separation-Mediated TARP/MAGUK Complex Condensation and AMPA Receptor Synaptic Transmission
Zeng, M., Díaz-Alonso, J., Ye, F., Chen, X., Xu, J., Ji, Z., Nicoll, R. A., & Zhang, M. (2019) · Neuron · doi:10.1016/j.neuron.2019.08.001 · Cited by 171 · see citing works
Mechanisms of homeostatic plasticity in the excitatory synapse
Fernandes, D., & Carvalho, A. L. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13687 · Cited by 170 · see citing works
Twenty Years of SynGAP Research: From Synapses to Cognition
Gamache, T. R., Araki, Y., & Huganir, R. L. (2020) · The Journal of Neuroscience · doi:10.1523/jneurosci.0420-19.2020 · Cited by 161 · see citing works
Long-term potentiation: Peeling the onion
Nicoll, R. A., & Roche, K. W. (2013) · Neuropharmacology · doi:10.1016/j.neuropharm.2013.02.010 · Cited by 146 · see citing works
Insights into Rapid Modulation of Neuroplasticity by Brain Estrogens
Srivastava, D. P., Woolfrey, K. M., & Penzes, P. (2013) · Pharmacological Reviews · doi:10.1124/pr.111.005272 · Cited by 138 · see citing works
NMDAR-dependent long-term depression is associated with increased short term plasticity through autophagy mediated loss of PSD-95
Compans, B., Camus, C., Kallergi, E., Sposini, S., Martineau, M., Butler, C., Kechkar, A., Klaassen, R. V., Retailleau, N., B, T. J. S. A., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-23133-9 · Cited by 136 · see citing works
Self-citation
Synaptic memory and CaMKII
Nicoll, R. A., & Schulman, H. (2023) · Physiological Reviews · doi:10.1152/physrev.00034.2022 · Cited by 126 · see citing works
“It is now well established that the delivery of AMPARs to synapses requires the binding of TARPs, via their PDZ binding motifs (PBMs), to PSD-95 (278, 279, 286, 289, 294).”
Background
Plasticity of dendritic spines: subcompartmentalization of signaling
Colgan, L. A., & Yasuda, R. (2014) · Annual Review of Physiology · doi:10.1146/annurev-physiol-021113-170400 · Cited by 124 · see citing works
Optogenetic Control of Synaptic Composition and Function
Sinnen, B. L., Bowen, A. B., Forte, J. S., Hiester, B. G., Crosby, K. C., Gibson, E. S., Dell’Acqua, M. L., & Kennedy, M. J. (2017) · Neuron · doi:10.1016/j.neuron.2016.12.037 · Cited by 124 · see citing works
AMPA receptors and their minions: auxiliary proteins in AMPA receptor trafficking
Bissen, D., Foss, F., & Acker-Palmer, A. (2019) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03068-7 · Cited by 92 · see citing works
Phosphorylation-Dependent Regulation of Ca2+-Permeable AMPA Receptors During Hippocampal Synaptic Plasticity
Purkey, A., & Dell’Acqua, M. L. (2020) · Frontiers in Synaptic Neuroscience · doi:10.3389/fnsyn.2020.00008 · Cited by 113 · see citing works
Synaptic transmission and plasticity require AMPA receptor anchoring via its N-terminal domain
Watson, J. F., Ho, H., & Greger, I. H. (2017) · eLife · doi:10.7554/elife.23024 · Cited by 117 · see citing works
The Regulation of Synaptic Protein Turnover
Alvarez-Castelao, B., & Schuman, E. M. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.r115.657130 · Cited by 110 · see citing works
Shisa6 traps AMPA receptors at postsynaptic sites and prevents their desensitization during synaptic activity
Klaassen, R. V., Stroeder, J., Coussen, F., Hafner, A., Petersen, J. D., Renancio, C., Schmitz, L. J. M., Normand, E., Lodder, J. C., Rotaru, D. C., et al. (2016) · Nature Communications · doi:10.1038/ncomms10682 · Cited by 112 · see citing works
Self-citation
Lengthening of the Stargazin Cytoplasmic Tail Increases Synaptic Transmission by Promoting Interaction to Deeper Domains of PSD-95
Hafner, A.-S., Penn, A. C., Grillo-Bosch, D., Retailleau, N., Poujol, C., Philippat, A., Coussen, F., Sainlos, M., Opazo, P., & Choquet, D. (2015) · Neuron · doi:10.1016/j.neuron.2015.03.013 · Cited by 101 · see citing works
Self-citation
A Septin-Dependent Diffusion Barrier at Dendritic Spine Necks
Ewers, H., Tada, T., Petersen, J. D., Rácz, B., Sheng, M., & Choquet, D. (2014) · PLoS ONE · doi:10.1371/journal.pone.0113916 · Cited by 104 · see citing works
Self-citation
Intracellular oligomeric amyloid-beta rapidly regulates GluA1 subunit of AMPA receptor in the hippocampus
Whitcomb, D. J., Hogg, E. L., Regan, P. L., Piers, T. M., Narayan, P. S., Whitehead, G., Winters, B. L., Kim, D.-H., Kim, E., George‐Hyslop, P. S., et al. (2015) · Scientific Reports · doi:10.1038/srep10934 · Cited by 105 · see citing works
Neddylation inhibition impairs spine development, destabilizes synapses and deteriorates cognition
Vogl, A. M., Brockmann, M. M., Giusti, S. A., Maccarrone, G., Vercelli, C. A., Bauder, C. A., Richter, J. S., Roselli, F., Hafner, A., Dedic, N., et al. (2015) · Nature Neuroscience · doi:10.1038/nn.3912 · Cited by 99 · see citing works
Self-citation
SynGAP regulates synaptic plasticity and cognition independently of its catalytic activity
Araki, Y., Rajkovich, K. E., Gerber, E. E., Gamache, T. R., Johnson, R. C., Tran, T. H. N., Liu, B., Zhu, Q., Hong, I., Kirkwood, A., et al. (2024) · Science · doi:10.1126/science.adk1291 · Cited by 92 · see citing works
Ouabain-Induced Cochlear Nerve Degeneration: Synaptic Loss and Plasticity in a Mouse Model of Auditory Neuropathy
Yuan, Y.-S., Shi, F., Yin, Y., Tong, M., Lang, H., Polley, D. B., Liberman, M. C., & Edge, A. S. B. (2013) · Journal of the Association for Research in Otolaryngology · doi:10.1007/s10162-013-0419-7 · Cited by 96 · see citing works
Subsynaptic positioning of AMPARs by LRRTM2 controls synaptic strength
Ramsey, A. M., Tang, A., LeGates, T. A., Gou, X., Carbone, B. E., Thompson, S. M., Biederer, T., & Blanpied, T. A. (2021) · Science Advances · doi:10.1126/sciadv.abf3126 · Cited by 90 · see citing works
Scaffolding Proteins of the Post-synaptic Density Contribute to Synaptic Plasticity by Regulating Receptor Localization and Distribution: Relevance for Neuropsychiatric Diseases
Iasevoli, F., Tomasetti, C., & de Bartolomeis, A. (2012) · Neurochemical Research · doi:10.1007/s11064-012-0886-y · Cited by 88 · see citing works
Palmitoylation regulates glutamate receptor distributions in postsynaptic densities through control of PSD95 conformation and orientation
Jeyifous, O., Lin, E. I., Chen, X., Antinone, S. E., Mastro, R., Drisdel, R. C., Reese, T. S., & Green, W. N. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1612963113 · Cited by 89 · see citing works
Durable fear memories require PSD-95
Fitzgerald, P. J., Pinard, C. R., Camp, M., Feyder, M. J., Sah, A., Bergstrom, H. C., Graybeal, C., Liu, Y., Schlüter, O. M., Grant, S. G. N., et al. (2014) · Molecular Psychiatry · doi:10.1038/mp.2014.161 · Cited by 85 · see citing works
Huntingtin and the Synapse
Barron, J. C., Hurley, E. P., & Parsons, M. P. (2021) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2021.689332 · Cited by 85 · see citing works
Organization and dynamics of the actin cytoskeleton during dendritic spine morphological remodeling
Chazeau, A., & Giannone, G. (2016) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-016-2214-1 · Cited by 85 · see citing works
Synaptically released matrix metalloproteinase activity in control of structural plasticity and the cell surface distribution of GluA1-AMPA receptors
Szepesi, Z., Hosy, E., Ruszczycki, B., Bijata, M., Pyskaty, M., Bikbaev, A., Heine, M., Choquet, D., Kaczmarek, L., & Wlodarczyk, J. (2014) · PLoS ONE · doi:10.1371/journal.pone.0098274 · Cited by 83 · see citing works
Self-citation
Synaptic Consolidation Normalizes AMPAR Quantal Size following MAGUK Loss
Levy, J. M., Chen, X.-B., Reese, T., & Nicoll, R. (2015) · Neuron · doi:10.1016/j.neuron.2015.07.015 · Cited by 77 · see citing works
Subsynaptic spatial organization as a regulator of synaptic strength and plasticity
Chen, H., Tang, A., & Blanpied, T. A. (2018) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2018.05.004 · Cited by 84 · see citing works
Sevoflurane Acts on Ubiquitination–Proteasome Pathway to Reduce Postsynaptic Density 95 Protein Levels in Young Mice
Han, L., Liufu, N., Dong, Y., Xu, G., Zhang, Y., Shu, L., Soriano, S. G., Zheng, H., Yu, B., & Xie, Z. (2017) · Anesthesiology · doi:10.1097/aln.0000000000001889 · Cited by 81 · see citing works
A model for regulation by SynGAP-α1 of binding of synaptic proteins to PDZ-domain 'Slots' in the postsynaptic density
Walkup, W. G., Mastro, T. L., Schenker, L. T., Vielmetter, J., Hu, R., Iancu, A., Reghunathan, M., Bannon, B. D., & Kennedy, M. B. (2016) · eLife · doi:10.7554/elife.16813 · Cited by 76 · see citing works
Arc/Arg3.1 function in long‐term synaptic plasticity: Emerging mechanisms and unresolved issues
Zhang, H., & Bramham, C. R. (2020) · European Journal of Neuroscience · doi:10.1111/ejn.14958 · Cited by 71 · see citing works
Leucine-Rich Repeat Transmembrane Proteins Are Essential for Maintenance of Long-Term Potentiation
Soler-Llavina, G. J., Arstikaitis, P., Morishita, W., Ahmad, M., Südhof, T. C., & Malenka, R. C. (2013) · Neuron · doi:10.1016/j.neuron.2013.06.007 · Cited by 77 · see citing works
Synaptic Size Dynamics as an Effectively Stochastic Process
Statman, A., Kaufman, M., Minerbi, A., Ziv, N. E., & Brenner, N. (2014) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1003846 · Cited by 82 · see citing works
Super-resolution imaging of synaptic and Extra-synaptic AMPA receptors with different-sized fluorescent probes
Lee, S. H., Jin, C., Cai, E., Ge, P., Ishitsuka, Y., Teng, K. W., de Thomaz, A. A., Nall, D., Baday, M., Jeyifous, O., et al. (2017) · eLife · doi:10.7554/elife.27744 · Cited by 76 · see citing works
AMPA Receptors in Synaptic Plasticity, Memory Function, and Brain Diseases
de León-López, C. A. M., Carretero-Rey, M., & Khan, Z. U. (2025) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-024-01529-7 · Cited by 73 · see citing works
Ligand binding by PDZ domains
Celestine, N., Bach, A., Strømgaard, K., Gianni, S., & Jemth, P. (2012) · BioFactors · doi:10.1002/biof.1031 · Cited by 72 · see citing works
α2δ2 Controls the Function and Trans-Synaptic Coupling of Cav1.3 Channels in Mouse Inner Hair Cells and Is Essential for Normal Hearing
Fell, B., Eckrich, S., Blum, K., Eckrich, T., Hecker, D., Obermair, G. J., Münkner, S., Flockerzi, V., Schick, B., & Engel, J. (2016) · Journal of Neuroscience · doi:10.1523/jneurosci.3468-14.2016 · Cited by 68 · see citing works
The Regulation of AMPA Receptor Endocytosis by Dynamic Protein-Protein Interactions
Hanley, J. G. (2018) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2018.00362 · Cited by 67 · see citing works
Mapping the Interaction Sites between AMPA Receptors and TARPs Reveals a Role for the Receptor N-Terminal Domain in Channel Gating
Cais, O., Herguedas, B., Krol, K., Cull-Candy, S. G., Farrant, M., & Greger, I. H. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.09.029 · Cited by 67 · see citing works
Synaptic Targeting and Function of SAPAPs Mediated by Phosphorylation-Dependent Binding to PSD-95 MAGUKs
Zhu, J., Zhou, Q., Shang, Y., Li, H., Peng, M., Ke, X., Weng, Z., Zhang, R., Huang, X., Li, S. S. C., et al. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.11.107 · Cited by 68 · see citing works
AMPA receptor trafficking and LTP: Carboxy-termini, amino-termini and TARPs
Díaz-Alonso, J., & Nicoll, R. A. (2021) · Neuropharmacology · doi:10.1016/j.neuropharm.2021.108710 · Cited by 66 · see citing works
LTP requires postsynaptic PDZ-domain interactions with glutamate receptor/auxiliary protein complexes
Sheng, N., Bemben, M. A., Díaz-Alonso, J., Tao, W., Shi, Y. S., & Nicoll, R. A. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1800719115 · Cited by 65 · see citing works
Activity-dependent PI(3,5)P 2 synthesis controls AMPA receptor trafficking during synaptic depression
McCartney, A. J., Zolov, S. N., Kauffman, E. J., Zhang, Y., Strunk, B. S., Weisman, L. S., & Sutton, M. A. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1411117111 · Cited by 63 · see citing works
Synaptic activity regulates AMPA receptor trafficking through different recycling pathways
Zheng, N., Jeyifous, O., Munro, C., Montgomery, J. M., & Green, W. N. (2015) · eLife · doi:10.7554/elife.06878 · Cited by 59 · see citing works
β-Amyloid disruption of LTP/LTD balance is mediated by AKAP150-anchored PKA and Calcineurin regulation of Ca2+-permeable AMPA receptors
Sanderson, J. L., Freund, R. K., Gorski, J. A., & Dell’Acqua, M. L. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109786 · Cited by 60 · see citing works
Shape-induced asymmetric diffusion in dendritic spines allows efficient synaptic AMPA receptor trapping
Kusters, R., Kapitein, L. C., Hoogenraad, C. C., & Storm, C. (2013) · Biophysical Journal · doi:10.1016/j.bpj.2013.11.016 · Cited by 53 · see citing works
Nanoscale rules governing the organization of glutamate receptors in spine synapses are subunit specific
Hruska, M., Cain, R. E., & Dalva, M. B. (2022) · Nature Communications · doi:10.1038/s41467-022-28504-4 · Cited by 56 · see citing works
Synapse organizers as molecular codes for synaptic plasticity
Connor, S. A., & Siddiqui, T. J. (2023) · Trends in Neurosciences · doi:10.1016/j.tins.2023.08.001 · Cited by 59 · see citing works
A Novel Mechanism for Nicotinic Potentiation of Glutamatergic Synapses
Halff, A. W., Gómez‐Varela, D., John, D., & Berg, D. K. (2014) · Journal of Neuroscience · doi:10.1523/jneurosci.2795-13.2014 · Cited by 54 · see citing works
Synaptic adhesion molecule IgSF11 regulates synaptic transmission and plasticity
Jang, S., Oh, D., Lee, Y., Hosy, E., Shin, H., van Riesen, C., Whitcomb, D. J., Warburton, J. M., Jo, J., Kim, D., et al. (2015) · Nature Neuroscience · doi:10.1038/nn.4176 · Cited by 52 · see citing works
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Authors: Opazo, P., Sainlos, M., & Choquet, D.
Affiliations: Centre National de la Recherche Scientifique (FR)
Corresponding author: Choquet, Daniel
ORCID: Opazo, Patricio
Sainlos, Matthieu
Choquet, Daniel
Venue: Current Opinion in Neurobiology
Publisher: Elsevier BV
Published: 2012-06
Volume: 22
Issue: 3
Pages: 453-460
ISSN: 0959-4388 (ISSN-L)
DOI: 10.1016/j.conb.2011.10.010
OpenAlex: W1971924693
Cited by: 234
References: 98
Citations by year: 2026: 10 · 2025: 10 · 2024: 11 · 2023: 12 · 2022: 18 · 2021: 27 · 2020: 13 · 2019: 11 · 2018: 19 · 2017: 17 · 2016: 18 · 2015: 16 · 2014: 25 · 2013: 19 · 2012: 8
FWCI: 1.58
Type: journal article
Language: en
Open access: closed
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
Locations: Current Opinion in Neurobiology (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nicotinic Acetylcholine Receptors Study
Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genetics and Neurodevelopmental Disorders
Keywords: AMPA receptors, PSD-95, stargazin, postsynaptic density, long-term potentiation, synaptic plasticity, protein-protein interaction, activity-dependent regulation
MeSH terms: Animals, Synaptic Transmission, Synapses, Long-Term Potentiation, Receptors, AMPA, Protein Transport, Intracellular Signaling Peptides and Proteins

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Regulation of AMPA receptor surface diffusion by PSD-95 slots

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