Cited by 91Neuroscience and Neuropharmacology ResearchMemory and Neural MechanismsReceptor Mechanisms and Signaling

The δ2 glutamate receptor gates long-term depression by coordinating interactions between two AMPA receptor phosphorylation sites

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Kohda, Kazuhisa, Kakegawa, Wataru, Matsuda, Shinji, Yamamoto, Tadashi, Hirano, Hisashi, Yuzaki, Michisuke·2013·Proceedings of the National Academy of Sciences

Abstract

Significance: Long-term depression (LTD) commonly affects learning and memory in various brain regions. Although LTD in the cerebellum absolutely requires δ2 glutamate receptors, its underlying mechanisms remain elusive. LTD is caused by endocytosis of AMPA receptors, which is triggered by activity-induced serine phosphorylation of the GluA2 subunit. Our work showed that this serine phosphorylation required prior dephosphorylation of the nearby tyrosine residue. By interaction with a tyrosine phosphatase, δ2 glutamate receptors regulated tyrosine dephosphorylation status of GluA2 to gate inducibility of LTD. These findings will provide better understanding of general mechanisms regulating AMPA receptor endocytosis during synaptic plasticity.

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Crossref · 10.1073/pnas.1218380110

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  • Dephosphorylation of GluA2 Y876 by tyrosine phosphatase PTPMEG is necessary for S880 phosphorylation and expression of cerebellar LTD.

    “Dephosphorylation of GluA2 Y876 by tyrosine phosphatase PTPMEG was necessary for S880 phosphorylation and expression of cerebellar LTD (Kohda et al., 2013).”

    From The AMPA Receptor Code of Synaptic Plasticity (2018) · cites this paper as Kohda et al., 2013

  • In cerebellar Purkinje neurons, phosphorylation of GluA2 Y876 inhibits subsequent phosphorylation of GluA2 S880.

    “In cerebellar Purkinje neurons, phosphorylation of GluA2 Y876 has been shown to inhibit subsequent phosphorylation of GluA2 S880 (Figure 1) (Kohda et al., 2013).”

    From The AMPA Receptor Code of Synaptic Plasticity (2018) · cites this paper as Kohda et al., 2013

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Authors
Kohda, K., Kakegawa, W., Matsuda, S., Yamamoto, T., Hirano, H., & Yuzaki, M.
Affiliations
  • Keio University (JP)
  • Okinawa Institute of Science and Technology Graduate University (JP)
  • Yokohama City University (JP)
Venue
Proceedings of the National Academy of Sciences
Published
2013-02-19
Volume
110
Issue
10
Pages
E948-57
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W2052729994
Cited by
90
References
49
Citations by year
2025: 4 · 2024: 3 · 2023: 9 · 2022: 6 · 2021: 15 · 2020: 10 · 2019: 2 · 2018: 7 · 2017: 5 · 2016: 10 · 2015: 7 · 2014: 8 · 2013: 4
FWCI
4.74
Type
journal article
Language
en
Open access
Locations
  • Proceedings of the National Academy of Sciences (publishedVersion)
  • Europe PMC (PubMed Central) (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • Naito Foundation
  • Takeda Science Foundation
  • Keio University
  • Ministry of Education, Culture, Sports, Science and Technology (CREST)
  • Inamori Foundation
  • Japan Society for the Promotion of Science (21229006, 23500399, 23689012)
  • Japan Science and Technology Agency (CREST)
  • Core Research for Evolutional Science and Technology
  • Precursory Research for Embryonic Science and Technology
Topics
  • Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
  • Life Sciences › Neuroscience › Cognitive Neuroscience › Memory and Neural Mechanisms
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
Keywords
GluD2, long-term depression, AMPA receptors, GluA2, receptor internalization, Purkinje cells, cerebellum, dephosphorylation, synaptic plasticity
MeSH terms
ADP-Ribosylation Factor 6, Animals, Cerebellum, Models, Neurological, Neuronal Plasticity, Phosphorylation, Purkinje Cells, Serine, Tyrosine, Signal Transduction, Receptors, Glutamate, Receptors, AMPA, Mice, Knockout, Patch-Clamp Techniques, Guanine Nucleotide Exchange Factors, ADP-Ribosylation Factors, Protein Subunits, Long-Term Synaptic Depression, Mice, Protein Tyrosine Phosphatase, Non-Receptor Type 4, Protein Interaction Domains and Motifs

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