Cited by 567Neuroscience and Neuropharmacology ResearchUbiquitin and proteasome pathwaysGenetics and Neurodevelopmental Disorders

The DOI matches its Crossref record; 65 of the 65 references it cites were found in a registry or an index.

Ubiquitination Regulates PSD-95 Degradation and AMPA Receptor Surface Expression

Open access

Colledge, Marcie, Snyder, Eric M., Crozier, Robert A., Soderling, Jacquelyn A., Jin, Yetao, Langeberg, Lorene K., Lu, Hua, Bear, Mark F., Scott, John D.·2003·Neuron

DOI 10.1016/s0896-6273(03)00687-1PMC PMC3963808

Open this paper in CoChat — free account Open PDF

Abstract

PSD-95 is a major scaffolding protein of the postsynaptic density, tethering NMDA- and AMPA-type glutamate receptors to signaling proteins and the neuronal cytoskeleton. Here we show that PSD-95 is regulated by the ubiquitin-proteasome pathway. PSD-95 interacts with and is ubiquitinated by the E3 ligase Mdm2. In response to NMDA receptor activation, PSD-95 is ubiquitinated and rapidly removed from synaptic sites by proteasome-dependent degradation. Mutations that block PSD-95 ubiquitination prevent NMDA-induced AMPA receptor endocytosis. Likewise, proteasome inhibitors prevent NMDA-induced AMPA receptor internalization and synaptically induced long-term depression. This is consistent with the notion that PSD-95 levels are an important determinant of AMPA receptor number at the synapse. These data suggest that ubiquitination of PSD-95 through an Mdm2-mediated pathway is critical in regulating AMPA receptor surface expression during synaptic plasticity.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.1016/s0896-6273(03)00687-1

Cites

65 of 65 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Calcineurin is a common target of cyclophilin-cyclosporin A and FKBP-FK506 complexes
Liu, J., Farmer, J. D., Lane, W. S., Friedman, J., Weissman, I., & Schreiber, S. L. (1991) · Cell · doi:10.1016/0092-8674(91)90124-h · Cited by 4,116
AMPA Receptor Trafficking and Synaptic Plasticity
Malinow, R., & Malenka, R. C. (2002) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.25.112701.142758 · Cited by 2,588
Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53
Honda, R., Tanaka, H., & Yasuda, H. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)01480-4 · Cited by 1,951
PEST sequences and regulation by proteolysis
Rechsteiner, M., & Rogers, S. W. (1996) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(96)10031-1 · Cited by 1,707
Themes and variations on ubiquitylation
Weissman, A. M. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35056563 · Cited by 1,507
Rescue of early embryonic lethality in mdm2-deficient mice by deletion of p53
de Oca Luna, R. M., Wagner, D. S., & Lozano, G. (1995) · Nature · doi:10.1038/378203a0 · Cited by 1,420 · cited 2×
“We cotransfected from mice lacking Mdm2 (Montes de Oca Luna et al., 1995).”
Synaptic plasticity: LTP and LTD
Bear, M. F., & Malenka, R. C. (1994) · Current Opinion in Neurobiology · doi:10.1016/0959-4388(94)90101-5 · Cited by 1,355
Self-citation
PSD-95 Involvement in Maturation of Excitatory Synapses
El-Husseini, A. E.-D., Schnell, E., Chetkovich, D. M., Nicoll, R. A., & Bredt, D. S. (2000) · Science · doi:10.1126/science.290.5495.1364 · Cited by 1,303
Enhanced long-term potentiation and impaired learning in mice with mutant postsynaptic density-95 protein.
Migaud, M., Charlesworth, P., Dempster, M., Webster, L. C., Watabe, A. M., Makhinson, M., He, Y., Ramsay, M. F., Morris, R. G. M., Morrison, J. H., et al. (1998) · Nature · doi:10.1038/24790 · Cited by 1,160
Regulation of distinct AMPA receptor phosphorylation sites during bidirectional synaptic plasticity
Lee, H.-K., Barbarosie, M., Kameyama, K., Bear, M. F., & Huganir, R. L. (2000) · Nature · doi:10.1038/35016089 · Cited by 1,116
Self-citation

Show all 65 references

Sorted by citations

LTP and LTD
Malenka, R. C., & Bear, M. F. (2004) · Neuron · doi:10.1016/j.neuron.2004.09.012 · Cited by 3,968
Self-citation
Synaptic Plasticity: Multiple Forms, Functions, and Mechanisms
Citri, A., & Malenka, R. C. (2008) · Neuropsychopharmacology · doi:10.1038/sj.npp.1301559 · Cited by 2,323
PDZ domain proteins of synapses
Kim, E., & Sheng, M. (2004) · Nature reviews. Neuroscience · doi:10.1038/nrn1517 · Cited by 1,630
AKAP signalling complexes: focal points in space and time
Wong, W., & Scott, J. D. (2004) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1527 · Cited by 1,073
Self-citation
Receptor trafficking and synaptic plasticity
Collingridge, G. L., Isaac, J. T. R., & Wang, Y. T. (2004) · Nature Reviews Neuroscience · doi:10.1038/nrn1556 · Cited by 1,046
The Postsynaptic Architecture of Excitatory Synapses: A More Quantitative View
Sheng, M., & Hoogenraad, C. C. (2007) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.76.060805.160029 · Cited by 1,003
The cell biology of synaptic plasticity: AMPA receptor trafficking
Shepherd, J. D., & Huganir, R. L. (2007) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.23.090506.123516 · Cited by 978
Specificity in Signal Transduction
Pawson, T. J. (2004) · Cell · doi:10.1016/s0092-8674(03)01077-8 · Cited by 821
Postsynaptic BDNF‐TrkB signaling in synapse maturation, plasticity, and disease
Yoshii, A., & Constantine‐Paton, M. (2010) · Developmental Neurobiology · doi:10.1002/dneu.20765 · Cited by 744
The Postsynaptic Organization of Synapses
Sheng, M., & Kim, E. (2011) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a005678 · Cited by 603
Labelling and optical erasure of synaptic memory traces in the motor cortex
Hayashi-Takagi, A., Yagishita, S., Nakamura, M., Shirai, F., Wu, Y. I., Loshbaugh, A. L., Kuhlman, B., Hahn, K. M., & Kasai, H. (2015) · Nature · doi:10.1038/nature15257 · Cited by 624
Ubiquitin, the proteasome and protein degradation in neuronal function and dysfunction
Tai, H.-C., & Schuman, E. M. (2008) · Nature Reviews Neuroscience · doi:10.1038/nrn2499 · Cited by 532
Dynamic Translational and Proteasomal Regulation of Fragile X Mental Retardation Protein Controls mGluR-Dependent Long-Term Depression
Hou, L., Antion, M. D., Hu, D., Spencer, C. M., Paylor, R., & Klann, E. (2006) · Neuron · doi:10.1016/j.neuron.2006.07.005 · Cited by 469
PSD-95 is required for activity-driven synapse stabilization.
Ehrlich, I., Klein, M., Rumpel, S., & Malinow, R. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0609307104 · Cited by 470
Rapid Translation of Arc/Arg3.1 Selectively Mediates mGluR-Dependent LTD through Persistent Increases in AMPAR Endocytosis Rate
Waung, M. W., Pfeiffer, B. E., Nosyreva, E. D., Ronesi, J. A., & Huber, K. M. (2008) · Neuron · doi:10.1016/j.neuron.2008.05.014 · Cited by 474
MEMBRANE-ASSOCIATED GUANYLATE KINASES REGULATE ADHESION AND PLASTICITY AT CELL JUNCTIONS
Funke, L., Dakoji, S., & Bredt, D. S. (2005) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.74.082803.133339 · Cited by 482
Dysregulated Metabotropic Glutamate Receptor-Dependent Translation of AMPA Receptor and Postsynaptic Density-95 mRNAs at Synapses in a Mouse Model of Fragile X Syndrome
Muddashetty, R. S., Kelić, S., Gross, C., Xu, M., & Bassell, G. J. (2007) · The Journal of Neuroscience · doi:10.1523/jneurosci.0937-07.2007 · Cited by 421
The Angelman syndrome ubiquitin ligase localizes to the synapse and nucleus, and maternal deficiency results in abnormal dendritic spine morphology
Dindot, S. V., Antalffy, B. A., Bhattacharjee, M. B., & Beaudet, A. L. (2007) · Human Molecular Genetics · doi:10.1093/hmg/ddm288 · Cited by 418
Deubiquitylases From Genes to Organism
Clague, M. J., Barsukov, I., Coulson, J. M., Liu, H., Rigden, D. J., & Urbé, S. (2013) · Physiological Reviews · doi:10.1152/physrev.00002.2013 · Cited by 439
Linking neurodevelopmental and synaptic theories of mental illness through DISC1
Brandon, N. J., & Sawa, A. (2011) · Nature reviews. Neuroscience · doi:10.1038/nrn3120 · Cited by 431
Regulation of hippocampal synaptic plasticity by BDNF
Leal, G., Afonso, P. M., Salazar, I. L., & Duarte, C. B. (2015) · Brain Research · doi:10.1016/j.brainres.2014.10.019 · Cited by 410
MECHANISMS OF VERTEBRATE SYNAPTOGENESIS
Waites, C. L., Craig, A. M., & Garner, C. C. (2005) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.27.070203.144336 · Cited by 483
Beta-amyloid accumulation in APP mutant neurons reduces PSD-95 and GluR1 in synapses
Almeida, C. G., Tampellini, D., Takahashi, R. H., Greengard, P., Lin, M. T., Snyder, E. M., & Gouras, G. K. (2005) · Neurobiology of Disease · doi:10.1016/j.nbd.2005.02.008 · Cited by 397
Self-citation
Mitochondrial Trafficking to Synapses in Cultured Primary Cortical Neurons
Chang, D. T. W., Honick, A. S., & Reynolds, I. J. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.1012-06.2006 · Cited by 391
Metabotropic Glutamate Receptor Activation Regulates Fragile X Mental Retardation Protein and Fmr1 mRNA Localization Differentially in Dendrites and at Synapses
Antar, L. N., Afroz, R., Dictenberg, J. B., Carroll, R. C., & Bassell, G. J. (2004) · The Journal of Neuroscience · doi:10.1523/jneurosci.0099-04.2004 · Cited by 411
Reversible Inhibition of PSD-95 mRNA Translation by miR-125a, FMRP Phosphorylation, and mGluR Signaling
Muddashetty, R. S., Nalavadi, V. C., Gross, C., Yao, X., Xing, L., Laur, O., Warren, S. T., & Bassell, G. J. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.05.006 · Cited by 364
Homeostatic plasticity and NMDA receptor trafficking
Pérez-Otaño, I., & Ehlers, M. D. (2005) · Trends in Neurosciences · doi:10.1016/j.tins.2005.03.004 · Cited by 356
BDNF Induces Transport of PSD-95 to Dendrites Through PI3K-AKT Signaling After NMDA Receptor Activation
Yoshii, A., & Constantine-Paton, M. (2007) · Nature Neuroscience · doi:10.1038/nn1903 · Cited by 345
Activity-dependent dynamics and sequestration of proteasomes in dendritic spines
Bingol, B., & Schuman, E. M. (2006) · Nature · doi:10.1038/nature04769 · Cited by 347
ORGANELLES AND TRAFFICKING MACHINERY FOR POSTSYNAPTIC PLASTICITY
Kennedy, M. J., & Ehlers, M. D. (2006) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.29.051605.112808 · Cited by 346
Rapid Redistribution of Synaptic PSD-95 in the Neocortex In Vivo
Gray, N. W., Weimer, R. M., Bureau, I., & Svoboda, K. (2006) · PLoS Biology · doi:10.1371/journal.pbio.0040370 · Cited by 350
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
Ube3a is required for experience-dependent maturation of the neocortex
Yashiro, K., Riday, T. T., Condon, K. H., Roberts, A. C., Bernardo, D. R., Prakash, R., Weinberg, R. J., Ehlers, M. D., & Philpot, B. D. (2009) · Nature Neuroscience · doi:10.1038/nn.2327 · Cited by 328
Delayed Stabilization of Dendritic Spines in Fragile X Mice
Cruz-Martin, A., Crespo, M., & Portera-Cailliau, C. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.0577-10.2010 · Cited by 321
NS21: Re-defined and modified supplement B27 for neuronal cultures
Chen, Y., Stevens, B., Chang, J., Milbrandt, J., Barres, B. A., & Hell, J. W. (2008) · Journal of Neuroscience Methods · doi:10.1016/j.jneumeth.2008.03.013 · Cited by 309
Organization 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 299
A Balance of Protein Synthesis and Proteasome-Dependent Degradation Determines the Maintenance of LTP
Fonseca, R., Vabulas, R. M., Hartl, F. U., Bonhoeffer, T., & Nägerl, U. V. (2006) · Neuron · doi:10.1016/j.neuron.2006.08.015 · Cited by 310
Synaptic Accumulation of PSD-95 and Synaptic Function Regulated by Phosphorylation of Serine-295 of PSD-95
Kim, M. J., Futai, K., Jo, J., Hayashi, Y., Cho, K., & Sheng, M. (2007) · Neuron · doi:10.1016/j.neuron.2007.09.007 · Cited by 278
Soluble β-Amyloid1-40Induces NMDA-Dependent Degradation of Postsynaptic Density-95 at Glutamatergic Synapses
Roselli, F., Tirard, M., Lu, J., Hutzler, P., Lamberti, P., Livrea, P., Morabito, M. A., & Almeida, O. F. X. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.3034-05.2005 · Cited by 284
Deconstruction for Reconstruction: The Role of Proteolysis in Neural Plasticity and Disease
Bingol, B., & Sheng, M. (2011) · Neuron · doi:10.1016/j.neuron.2010.11.006 · Cited by 275
Architecture of the Mouse Brain Synaptome
Zhu, F., Cizeron, M., Qiu, Z., Benavides‐Piccione, R., Kopanitsa, M. V., Skene, N., Koniaris, B., DeFelipe, J., Fransén, E. A., Komiyama, N. H., et al. (2018) · Neuron · doi:10.1016/j.neuron.2018.07.007 · Cited by 272
Subunit Rules Governing the Sorting of Internalized AMPA Receptors in Hippocampal Neurons
Lee, S. H., Simonetta, A., & Sheng, M. (2004) · Neuron · doi:10.1016/j.neuron.2004.06.015 · Cited by 268
Autophosphorylated CaMKIIα Acts as a Scaffold to Recruit Proteasomes to Dendritic Spines
Bingol, B., Wang, C.-F., Arnott, D., Cheng, D., Peng, J., & Sheng, M. (2010) · Cell · doi:10.1016/j.cell.2010.01.024 · Cited by 268
Ubiquitination in postsynaptic function and plasticity
Mabb, A. M., & Ehlers, M. D. (2010) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-100109-104129 · Cited by 255
Neuronal LRP1 Functionally Associates with Postsynaptic Proteins and Is Required for Normal Motor Function in Mice
May, P., Rohlmann, A., Bock, H. H., Zurhove, K., Marth, J. D., Schomburg, E. D., Noebels, J. L., Beffert, U., Sweatt, J. D., Weeber, E. J., et al. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.20.8872-8883.2004 · Cited by 236
Regulation of the proteasome by neuronal activity and calcium/calmodulin-dependent protein kinase II
Djakovic, S. N., Schwarz, L. A., Barylko, B., DeMartino, G. N., & Patrick, G. N. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.021956 · Cited by 236
AMPA receptor trafficking and the mechanisms underlying synaptic plasticity and cognitive aging
Henley, J. M., & Wilkinson, K. A. (2013) · Dialogues in Clinical Neuroscience · doi:10.31887/dcns.2013.15.1/jhenley · Cited by 242
The DLGAP family: neuronal expression, function and role in brain disorders
Rasmussen, A. H., Rasmussen, H. B., & Silahtaroglu, A. (2017) · Molecular Brain · doi:10.1186/s13041-017-0324-9 · Cited by 234
An SCF-like ubiquitin ligase complex that controls presynaptic differentiation
Liao, E. H., Hung, W., Abrams, B. S., & Zhen, M. (2004) · Nature · doi:10.1038/nature02647 · Cited by 233
Cdk5: a multifaceted kinase in neurodegenerative diseases
Cheung, Z. H., & Ip, N. Y. (2012) · Trends in Cell Biology · doi:10.1016/j.tcb.2011.11.003 · Cited by 233
Neuregulin 1 Promotes Excitatory Synapse Development and Function in GABAergic Interneurons
Ting, A. K. L., Chen, Y., Wen, L., Yin, D., Shen, C., Tao, Y., Liu, X., Xiong, W., & Mei, L. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.2538-10.2011 · Cited by 221
Excitation control: balancing PSD-95 function at the synapse
Keith, D. J. (2008) · Frontiers in Molecular Neuroscience · doi:10.3389/neuro.02.004.2008 · Cited by 223
Role of Ubiquitylation in Cellular Membrane Transport
Staub, O., & Rotin, D. (2006) · Physiological Reviews · doi:10.1152/physrev.00020.2005 · Cited by 218
Posttranslational regulation of AMPA receptor trafficking and function
Lü, W., & Roche, K. W. (2011) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2011.09.008 · Cited by 203
Molecular dissociation of the role of PSD-95 in regulating synaptic strength and LTD.
Xu, W., Schlüter, O. M., Steiner, P., Czervionke, B. L., Sabatini, B., & Malenka, R. C. (2008) · Neuron · doi:10.1016/j.neuron.2007.11.027 · Cited by 193
Emerging Roles for Ubiquitin and Protein Degradation in Neuronal Function
Yi, J. J., & Ehlers, M. D. (2007) · Pharmacological Reviews · doi:10.1124/pr.59.1.4 · Cited by 224
MAGUKs, Synaptic Development, and Synaptic Plasticity
Zheng, C.-Y., Seabold, G. K., Hořák, M., & Petralia, R. S. (2011) · The Neuroscientist · doi:10.1177/1073858410386384 · Cited by 201
Protein homeostasis and synaptic plasticity
Cajigas, I. J., Will, T. J., & Schuman, E. M. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.173 · Cited by 192
A critical role for PSD-95/AKAP interactions in endocytosis of synaptic AMPA receptors
Bhattacharyya, S., Biou, V., Xu, W., Schlüter, O., & Malenka, R. C. (2009) · Nature Neuroscience · doi:10.1038/nn.2249 · Cited by 185
Developmental Switch in Synaptic Mechanisms of Hippocampal Metabotropic Glutamate Receptor-Dependent Long-Term Depression
Nosyreva, E. D., & Huber, K. M. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.3652-04.2005 · Cited by 186
APCCdh1 mediates EphA4-dependent downregulation of AMPA receptors in homeostatic plasticity
Fu, A. K. Y., Hung, K.-W., Fu, W., Shen, C., Chen, Y., Xia, J., Lai, K., & Ip, N. Y. (2010) · Nature Neuroscience · doi:10.1038/nn.2715 · Cited by 184
A‐kinase anchoring proteins: From protein complexes to physiology and disease
Carnegie, G. K., Means, C. K., & Scott, J. D. (2009) · IUBMB Life · doi:10.1002/iub.168 · Cited by 186
Self-citation
Opposing effects of PSD‐93 and PSD‐95 on long‐term potentiation and spike timing‐dependent plasticity
Carlisle, H. J., Fink, A. E., Grant, S. G. N., & O’Dell, T. J. (2008) · The Journal of Physiology · doi:10.1113/jphysiol.2008.163469 · Cited by 172
PSD-95-like membrane associated guanylate kinases (PSD-MAGUKs) and synaptic plasticity
Xu, W. (2011) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2011.03.001 · Cited by 171
Impaired ubiquitin–proteasome system activity in the synapses of Huntington's disease mice
Wang, J., Wang, C.-E., Orr, A. L., Tydlacka, S., Li, S., & Li, X. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200709080 · Cited by 170
The Anaphase-Promoting Complex Regulates the Abundance of GLR-1 Glutamate Receptors in the Ventral Nerve Cord of C. elegans
Juo, P., & Kaplan, J. M. (2004) · Current Biology · doi:10.1016/j.cub.2004.11.010 · Cited by 164
Synaptic adhesion molecules and PSD-95
Han, K., & Kim, E. (2007) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2007.10.011 · Cited by 169
Identification of long-lived synaptic proteins by proteomic analysis of synaptosome protein turnover
Heo, S., Diering, G. H., Na, C. H., Nirujogi, R. S., Bachman, J. L., Pandey, A., & Huganir, R. L. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1720956115 · Cited by 168
PICK1 is a calcium‐sensor for NMDA‐induced AMPA receptor trafficking
Hanley, J. G., & Henley, J. M. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600801 · Cited by 162
Involvement of Protein Synthesis and Degradation in Long-Term Potentiation of Schaffer Collateral CA1 Synapses
Karpova, A., Mikhaylova, M., Thomas, U., Knöpfel, T., & Behnisch, T. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.4573-05.2006 · Cited by 162
Copper: from neurotransmission to neuroproteostasis
Opazo, C., Greenough, M. A., & Bush, A. I. (2014) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2014.00143 · Cited by 159
Nedd4‐mediated AMPA receptor ubiquitination regulates receptor turnover and trafficking
Lin, A. W., Hou, Q., Jarzylo, L. A., Amato, S., Gilbert, J. P., Shang, F., & Man, H. (2011) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07221.x · Cited by 161
Routes, destinations and delays: recent advances in AMPA receptor trafficking
Henley, J. M., Barker, E. A., & Glebov, O. O. (2011) · Trends in Neurosciences · doi:10.1016/j.tins.2011.02.004 · Cited by 173
Activity-dependent NMDA receptor degradation mediated by retrotranslocation and ubiquitination
Kato, A., Rouach, N., Nicoll, R. A., & Bredt, D. S. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0501769102 · Cited by 154
The ubiquitin-proteasome pathway and synaptic plasticityPreprint
Hegde, A. N. (2010) · Learning & Memory · doi:10.1101/lm.1504010 · Cited by 156
Protein quality control in Alzheimer's disease by the ubiquitin proteasome system
de Vrij, F. M. S., Fischer, D. F., VANLEEUWEN, F., & Hol, E. M. (2004) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2004.10.001 · Cited by 155
Ubiquitin and Protein Turnover in Synapse Function
Yi, J. J., & Ehlers, M. (2005) · Neuron · doi:10.1016/j.neuron.2005.07.008 · Cited by 150
Calpain and Synaptic Function
Wu, H., & Lynch, D. R. (2006) · Molecular Neurobiology · doi:10.1385/mn:33:3:215 · Cited by 155
Human Immunodeficiency Virus Protein Tat Induces Synapse Loss via a Reversible Process That Is Distinct from Cell Death
Kim, H. J., Martemyanov, K. A., & Thayer, S. A. (2008) · Journal of Neuroscience · doi:10.1523/jneurosci.2958-08.2008 · Cited by 150
Dual role of the exocyst in AMPA receptor targeting and insertion into the postsynaptic membrane
Gerges, N. Z., Backos, D. S., Rupasinghe, C. N., Spaller, M. R., & Esteban, J. A. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601065 · Cited by 147
Stress-induced NLRP3 inflammasome activation negatively regulates fear memory in mice
Dong, Y., Li, S., Lu, Y., Li, X., Liao, Y., Peng, Z., Li, Y., Hou, L., Yuan, Z., & Cheng, J. (2020) · Journal of Neuroinflammation · doi:10.1186/s12974-020-01842-0 · Cited by 148
Ubiquitin-proteasome-mediated local protein degradation and synaptic plasticity
Hegde, A. N. (2004) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2004.05.005 · Cited by 143
Discrete synaptic states define a major mechanism of synapse plasticity
Montgomery, J. M., & Madison, D. V. (2004) · Trends in Neurosciences · doi:10.1016/j.tins.2004.10.006 · Cited by 158
Regulation of Synaptic Structure by Ubiquitin C-Terminal Hydrolase L1
Cartier, A. E., Djakovic, S. N., Salehi, A., Wilson, S. M., Masliah, E., & Patrick, G. N. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.1817-09.2009 · Cited by 141
Characterization of the brain 26S proteasome and its interacting proteins
Tai, H. (2010) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2010.00012 · Cited by 137
cAMP-Dependent Protein Kinase Postsynaptic Localization Regulated by NMDA Receptor Activation through Translocation of an A-Kinase Anchoring Protein Scaffold Protein
Smith, K. E., Gibson, E. S., & Dell’Acqua, M. L. (2006) · The Journal of Neuroscience · doi:10.1523/jneurosci.3092-05.2006 · Cited by 141
The psychiatric disease risk factors DISC1 and TNIK interact to regulate synapse composition and function
Wang, Q., Charych, E. I., Pulito, V., Lee, J., Graziane, N., Crozier, R., Revilla-Sánchez, R., Kelly, M. P., Dunlop, A. J., Murdoch, H., et al. (2010) · Molecular Psychiatry · doi:10.1038/mp.2010.87 · Cited by 164
Self-citation
Activity-Independent Regulation of Dendrite Patterning by Postsynaptic Density Protein PSD-95
Charych, E. I., Akum, B. F., Goldberg, J. S., Jörnsten, R. J., Rongo, C., Zheng, J. Q., & Firestein, B. L. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.2379-06.2006 · Cited by 141
AKAP150-Anchored Calcineurin Regulates Synaptic Plasticity by Limiting Synaptic Incorporation of Ca2+-Permeable AMPA Receptors
Sanderson, J. L., Gorski, J. A., Gibson, E. S., Lam, P., Freund, R. K., Chick, W. S., & Dell'Acqua, M. L. (2012) · The Journal of Neuroscience · doi:10.1523/jneurosci.3326-12.2012 · Cited by 137
“In particular, NMDA-cLTD activation of CaN and PP1/2A negatively regulates PSD-95 postsynaptic clustering and binding to Stargazin to promote AMPAR removal (Colledge et al., 2003; Tomita et al., 2005; Kim et al., 2007; Opazo et al., 2010).”
Background
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 144
A reduced number of metabotropic glutamate subtype 5 receptors are associated with constitutive homer proteins in a mouse model of fragile X syndrome
Giuffrida, R., Musumeci, S., D'Antoni, S., Bonaccorso, C. M., Giuffrida-Stella, A. M., Oostra, B. A., & Catania, M. V. (2005) · The Journal of Neuroscience · doi:10.1523/jneurosci.0932-05.2005 · Cited by 141
Ubiquitin pathways in neurodegenerative disease
Atkin, G., & Paulson, H. L. (2014) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2014.00063 · Cited by 140
Phosphorylation of Threonine-19 of PSD-95 by GSK-3 is Required for PSD-95 Mobilization and Long-Term Depression
Nelson, C. D., Kim, M. J., Hsin, H., Chen, Y., & Sheng, M. (2013) · Journal of Neuroscience · doi:10.1523/jneurosci.0131-13.2013 · Cited by 139
Role of the ubiquitin–proteasome system in brain ischemia: Friend or foe?
Caldeira, M. V., Salazar, I. L., Curcio, M., Canzoniero, L. M. T., & Duarte, C. B. (2013) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2013.10.003 · Cited by 135
PSD-95 and PSD-93 Play Critical But Distinct Roles in Synaptic Scaling Up and Down
Sun, Q., & Turrigiano, G. G. (2011) · The Journal of Neuroscience · doi:10.1523/jneurosci.5616-10.2011 · Cited by 135
Synaptic protein degradation by the ubiquitin proteasome system
Bingol, B., & Schuman, E. M. (2005) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2005.08.016 · Cited by 129
The ubiquitin–proteasome system as a critical regulator of synaptic plasticity and long-term memory formation
Jarome, T. J., & Helmstetter, F. J. (2013) · Neurobiology of Learning and Memory · doi:10.1016/j.nlm.2013.03.009 · Cited by 140
Dephosphorylation-Induced Ubiquitination and Degradation of FMRP in Dendrites: A Role in Immediate Early mGluR-Stimulated Translation
Nalavadi, V. C., Muddashetty, R. S., Gross, C., & Bassell, G. J. (2012) · The Journal of Neuroscience · doi:10.1523/jneurosci.5057-11.2012 · Cited by 128
UBE3A Regulates Synaptic Plasticity and Learning and Memory by Controlling SK2 Channel Endocytosis
Sun, J., Zhu, G., Liu, Y., Standley, S., Ji, A., Tunuguntla, R., Wang, Y., Claus, C., Luo, Y., Baudry, M., et al. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.06.023 · Cited by 131
Activity-Dependent Ubiquitination of GABAAReceptors Regulates Their Accumulation at Synaptic Sites
Saliba, R. S., Michels, G., Jacob, T. C., Pangalos, M. N., & Moss, S. J. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.3277-07.2007 · Cited by 133

Authors: Colledge, M., Snyder, E. M., Crozier, R. A., Soderling, J. A., Jin, Y., Langeberg, L. K., Lu, H., Bear, M. F., & Scott, J. D.
Affiliations: Howard Hughes Medical Institute (US)
Oregon Health & Science University (US)
Corresponding author: Scott, John D.
ORCID: Crozier, Robert A.
Langeberg, Lorene K.
Lu, Hua
Bear, Mark F.
Scott, John D.
Venue: Neuron
Publisher: Elsevier BV
Published: 2003-10
Volume: 40
Issue: 3
Pages: 595-607
ISSN: 0896-6273 (ISSN-L)
DOI: 10.1016/s0896-6273(03)00687-1
PMC: PMC3963808
OpenAlex: W2151538478
Cited by: 567
References: 65
Citations by year: 2026: 8 · 2025: 16 · 2024: 20 · 2023: 11 · 2022: 12 · 2021: 24 · 2020: 20 · 2019: 23 · 2018: 18 · 2017: 21 · 2016: 20 · 2015: 36 · 2014: 22 · 2013: 30 · 2012: 26
FWCI: 9.49
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 3577 d)
Locations: Neuron (publishedVersion)
PubMed (publishedVersion)
Europe PMC (PubMed Central) (acceptedVersion)
PubMed Central (acceptedVersion)
Funders: National Institute of General Medical Sciences (R01GM048231, GM-48231, R37GM048231)
National Institute of Neurological Disorders and Stroke (NS 39321, P01NS039321)
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genetics and Neurodevelopmental Disorders
Keywords: PSD-95, ubiquitination, MDM2, proteasomal degradation, AMPA receptors, receptor internalization, NMDA receptor activation, postsynaptic density, synaptic plasticity, long-term depression, glutamate receptors
MeSH terms: Disks Large Homolog 4 Protein, Acetylcysteine, Analysis of Variance, Animals, Animals, Newborn, Epitopes, Calcium, Cells, Cultured, Drug Interactions, Electric Stimulation, Embryo, Mammalian, Endocytosis, Colforsin, Hippocampus, Humans, Immunoglobulin G, Immunohistochemistry, Immunosuppressive Agents, Kidney, Leupeptins, Membrane Potentials, Membrane Proteins, Mutation, Nerve Tissue Proteins, Neural Inhibition, Neurons, Nuclear Proteins, Proto-Oncogene Proteins, Synapses, Time Factors, Transfection, Blotting, Western, Cysteine Proteinase Inhibitors, N-Methylaspartate, Tacrolimus, Synapsins, Receptors, AMPA, Patch-Clamp Techniques, Excitatory Amino Acid Agonists, Rats, Long-Evans, Ubiquitin, Intracellular Signaling Peptides and Proteins, Rats, Proto-Oncogene Proteins c-mdm2, In Vitro Techniques

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Ubiquitination Regulates PSD-95 Degradation and AMPA Receptor Surface Expression

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks