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Cited by 91Neuroscience and Neuropharmacology ResearchEpilepsy research and treatmentGenetics and Neurodevelopmental Disorders

LGI1–ADAM22–MAGUK configures transsynaptic nanoalignment for synaptic transmission and epilepsy prevention

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Fukata, Yuko, Chen, Xiumin, Chiken, Satomi, Hirano, Yoko, Yamagata, Atsushi, Inahashi, Hiroki, Sanbo, Makoto, Sano, Hiromi +8 more·2021·Proceedings of the National Academy of Sciences
DOI 10.1073/pnas.2022580118PMC PMC7826393
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Abstract

Significance: This study addresses a fundamental question in neuroscience, namely how does the presynaptic component of the synapse precisely align with the postsynaptic component? This is essential for the proper transmission of signals across the synapse. This paper focuses on a set of transsynaptic, epilepsy-related proteins that are essential for this alignment. We show that the LGI1–ADAM22–MAGUK complex is a key player in the nanoarchitecture of the synapse, such that the release site is directly apposed to the nanocluster of glutamate receptors.

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  • AMPARs form discrete clusters scattered around the PSD.

    “AMPARs form discrete clusters scattered around the PSD (256–259).”

    From Synaptic memory and CaMKII (2023) · cites this paper as [258]

    The Discussion states that AMPARs are present in the PSD and describes their capture through PSD-95. The Results describe discrete postsynaptic nanodomains of PSD-95, not AMPARs; our copy does not establish that AMPARs themselves form discrete clusters scattered around the PSD. (LLM, conf=0.82)

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Research works printed but not linked: 46

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Authors
Fukata, Y., Chen, X., Chiken, S., Hirano, Y., Yamagata, A., Inahashi, H., Sanbo, M., Sano, H., Goto, T., Hirabayashi, M., Kornau, H.-C., Prüss, H., Nambu, A., Fukai, S., Nicoll, R. A., & Fukata, M.
Affiliations
  • National Institutes of Natural Sciences (JP)
  • University of California, San Francisco (US)
  • RIKEN Center for Biosystems Dynamics Research (JP)
  • German Center for Neurodegenerative Diseases (DE)
  • Kyoto University (JP)
Corresponding author
  • Nicoll, Roger A.
  • Fukata, Masaki
ORCID
Venue
Proceedings of the National Academy of Sciences
Publisher
National Academy of Sciences
Published
2021-01-04
Volume
118
Issue
3
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
DOI
10.1073/pnas.2022580118
PMC
PMC7826393
OpenAlex
W3120307467
Cited by
91
References
5
Citations by year
2026: 7 · 2025: 14 · 2024: 28 · 2023: 12 · 2022: 15 · 2021: 15
FWCI
8.07
Type
journal article
Language
en
Open access
Licence
Locations
  • Proceedings of the National Academy of Sciences (publishedVersion, cc-by-nc-nd)
  • Europe PMC (PubMed Central) (publishedVersion, cc-by-nc-nd)
  • PubMed Central (publishedVersion, cc-by-nc-nd)
  • PubMed (publishedVersion)
  • Institutional Repositories DataBase (IRDB) (submittedVersion, cc-by-nc-nd)
  • DZNE Pub (submittedVersion)
  • Kyoto University Research Information Repository (Kyoto University) (submittedVersion, cc-by-nc-nd)
Funders
  • Ministry of Education, Culture, Sports, Science and Technology (19H03331, 19K22439, 19H03162, 15H05873, 18H03983, 19H04974, 19K22548, 20H04915, 20H00459)
  • HHS | National Institutes of Health (R01MH117139)
Topics
  • Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
  • Health Sciences › Medicine › Psychiatry and Mental health › Epilepsy research and treatment
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genetics and Neurodevelopmental Disorders
Keywords
LGI1, ADAM22, membrane-associated guanylate kinase, PSD-95, synaptic transmission, epilepsy, AMPA receptor potentiation, hippocampus, knock-in mice
MeSH terms
Animals, Brain, Calcium-Binding Proteins, Disease Models, Animal, Epilepsy, Hippocampus, Humans, Membrane Proteins, Nerve Tissue Proteins, Synaptic Transmission, Receptors, N-Methyl-D-Aspartate, Receptors, AMPA, Neural Cell Adhesion Molecules, Intracellular Signaling Peptides and Proteins, Mice, Guanylate Kinases, Shaker Superfamily of Potassium Channels, ADAM Proteins, Gene Knock-In Techniques

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