Evidence map›Paper›PMID 37884493›Full record

ArticleNature communications2023

GSG1L-containing AMPA receptor complexes are defined by their spatiotemporal expression, native interactome and allosteric sites.

Amanda M Perozzo, Jochen Schwenk, Aichurok Kamalova, Terunaga Nakagawa, Bernd Fakler, Derek Bowie

Abstract read
In one paragraph

Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

10 citing papers in PubMed.

  1. Review
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors.

Amanda M PerozzoIntegrated Program in Neuroscience, McGill University, Montreal, QC, H3A 1A1, Canada.ORCID 0000-0001-9681-3548
Jochen SchwenkInstitute of Physiology, Faculty of Medicine, University of Freiburg, Hermann-Herder-Str. 7, 79104, Freiburg, Germany.ORCID 0000-0003-3664-9795
Aichurok KamalovaDepartment of Molecular Physiology and Biophysics, Vanderbilt Brain Institute, Vanderbilt University School of Medicine, Nashville, TN, 37232, USA.
Terunaga NakagawaDepartment of Molecular Physiology and Biophysics, Vanderbilt Brain Institute, Vanderbilt University School of Medicine, Nashville, TN, 37232, USA.
Bernd FaklerInstitute of Physiology, Faculty of Medicine, University of Freiburg, Hermann-Herder-Str. 7, 79104, Freiburg, Germany.ORCID 0000-0001-7264-6423
Derek BowieDepartment of Pharmacology and Therapeutics, McGill University, Montreal, QC, H3G 1Y6, Canada. derek.bowie@mcgill.ca.ORCID 0000-0001-9491-8768

Funding

Mechanism of functional modulation of glutamate receptors by their auxiliary subunitsR01MH123474 · NIMH · VANDERBILT UNIVERSITY · PI Terunaga Nakagawa · 2022 to 2026
$2.3M
Molecular Anatomy of Mature and Immature Glutamate ReceptorsR01HD061543 · NICHD · VANDERBILT UNIVERSITY · PI NAKAGAWA, TERUNAGA · 2010 to 2014
$1.5M
Mechanism of functional modulation of glutamate receptors by their auxiliary subunitsR56MH123474 · NIMH · VANDERBILT UNIVERSITY · PI NAKAGAWA, TERUNAGA · 2020 to 2020
$383k
NICHD NIH HHS R01 HD061543NIMH NIH HHS R01 MH123474NIMH NIH HHS R56 MH123474
6 · The paper itself

Abstract

Transmembrane AMPA receptor regulatory proteins (TARPs) and germ cell-specific gene 1-like protein (GSG1L) are claudin-type AMPA receptor (AMPAR) auxiliary subunits that profoundly regulate glutamatergic synapse strength and plasticity. While AMPAR-TARP complexes have been extensively studied, less is known about GSG1L-containing AMPARs. Here, we show that GSG1L's spatiotemporal expression, native interactome and allosteric sites are distinct. GSG1L generally expresses late during brain development in a region-specific manner, constituting about 5% of all AMPAR complexes in adulthood. While GSG1L can co-assemble with TARPs or cornichons (CNIHs), it also assembles as the sole auxiliary subunit. Unexpectedly, GSG1L acts through two discrete evolutionarily-conserved sites on the agonist-binding domain with a weak allosteric interaction at the TARP/KGK site to slow desensitization, and a stronger interaction at a different site that slows recovery from desensitization. Together, these distinctions help explain GSG1L's evolutionary past and how it fulfills a unique signaling role within glutamatergic synapses.

Indexed as

ProteinsReceptors, AMPAAllosteric SiteSynapsesProteinsReceptors, AMPA

Identifiers

PMID37884493
PMCPMC10603098

What Socratic holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.