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

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Ubiquitination Regulates PSD-95 Degradation and AMPA Receptor Surface Expression

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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

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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.

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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

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Ubiquitination Regulates PSD-95 Degradation and AMPA Receptor Surface Expression

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