Cited by 441Neuroscience and Neuropharmacology ResearchCellular transport and secretionReceptor Mechanisms and Signaling

Clathrin adaptor AP2 and NSF interact with overlapping sites of GluR2 and play distinct roles in AMPA receptor trafficking and hippocampal LTD

Open access
Lee, Sang Hyoung, Liu, Lidong, Wang, Yu Tian, Sheng, Morgan·2002·Neuron

Abstract

Proteins that bind to the cytoplasmic tails of AMPA receptors control receptor trafficking and thus the strength of postsynaptic responses. Here we show that AP2, a clathrin adaptor complex important for endocytosis, associates with a region of GluR2 that overlaps the NSF binding site. Peptides used previously to interfere with NSF binding also antagonize GluR2-AP2 interaction. Using GluR2 mutants and peptide variants that dissociate NSF and AP2 interaction, we find that AP2 is involved specifically in NMDA receptor-induced (but not ligand-dependent) internalization of AMPA receptors, and is essential for hippocampal long-term depression (LTD). NSF function, on the other hand, is needed to maintain synaptic AMPA receptor responses, but is not directly required for NMDA receptor-mediated internalization and LTD.

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Crossref · 10.1016/s0896-6273(02)01024-3

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8 of 8 references verified0 citation errors · 0 not checkable

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  • GluA2 can directly interact with AP-2 clathrin adapter complex, which allows GluA2-containing receptors to be rapidly depleted from the cell-surface.

    “GluA2 can directly interact with AP-2 clathrin adapter complex, which allows GluA2-containing receptors to be rapidly depleted from the cell-surface (Kastning et al., 2007, Lee et al., 2002).”

    From The AMPA Receptor Code of Synaptic Plasticity (2018) · cites this paper as Lee et al., 2002

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Authors
Lee, S. H., Liu, L., Wang, Y. T., & Sheng, M.
Affiliations
  • Howard Hughes Medical Institute (US)
  • University of British Columbia (CA)
Corresponding author
Sheng, Morgan
Venue
Neuron
Publisher
Elsevier BV
Published
2002-11
Volume
36
Issue
4
Pages
661-674
ISSN
0896-6273 (ISSN-L)
OpenAlex
W2018775189
Cited by
441
References
8
Citations by year
2026: 4 · 2025: 2 · 2024: 8 · 2023: 4 · 2022: 7 · 2021: 13 · 2020: 15 · 2019: 9 · 2018: 17 · 2017: 15 · 2016: 17 · 2015: 11 · 2014: 18 · 2013: 19 · 2012: 20
FWCI
8.86
Type
journal article
Language
en
Open access
Locations
  • Neuron (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • EJLB Foundation
  • Canadian Institutes of Health Research
  • National Institutes of Health (NS35050)
Topics
  • Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
Keywords
AMPA receptor trafficking, GluR2, NSF, receptor internalization, synaptic plasticity, postsynaptic response
MeSH terms
Animals, Carrier Proteins, Cell Membrane, Endocytosis, Hippocampus, Synaptic Transmission, Neurons, Peptide Fragments, Synapses, Rats, Sprague-Dawley, Receptors, AMPA, Excitatory Amino Acid Agonists, Excitatory Postsynaptic Potentials, Protein Transport, Vesicular Transport Proteins, Adaptor Protein Complex 2, Long-Term Synaptic Depression, Rats, N-Ethylmaleimide-Sensitive Proteins

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