Evidence map›Paper›PMID 34678168›Full record

ArticleMolecular cell2021

Structure and desensitization of AMPA receptor complexes with type II TARP γ5 and GSG1L.

Oleg Klykov, Shanti Pal Gangwar, Maria V Yelshanskaya, Laura Yen, Alexander I Sobolevsky

Abstract read
In one paragraph

Article in Molecular cell, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing 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

35 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Review
  6. Article
  7. Molecular basis for ligand-gating of the human GluD1 receptor.bioRxiv : the preprint server for biology · 2026
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Efficient and rapid isolation of native AMPA receptor complexes for cryo-EM.Protein science : a publication of the Protein Society · 2026
    Article
  13. Article
  14. Article
  15. Activation of kainate receptor GluK2-Neto2 complex.Nature structural & molecular biology · 2025
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
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

5 authors.

Oleg KlykovDepartment of Biochemistry and Molecular Biophysics, Columbia University, 650 West 168th Street, New York, NY 10032, USA.
Shanti Pal GangwarDepartment of Biochemistry and Molecular Biophysics, Columbia University, 650 West 168th Street, New York, NY 10032, USA.
Maria V YelshanskayaDepartment of Biochemistry and Molecular Biophysics, Columbia University, 650 West 168th Street, New York, NY 10032, USA.
Laura YenDepartment of Biochemistry and Molecular Biophysics, Columbia University, 650 West 168th Street, New York, NY 10032, USA; Department of Physiology and Cellular Biophysics, Columbia University Irving Medical Center, 630 West 168th Street, New York, NY 10032, USA.
Alexander I SobolevskyDepartment of Biochemistry and Molecular Biophysics, Columbia University, 650 West 168th Street, New York, NY 10032, USA. Electronic address: as4005@cumc.columbia.edu.

Funding

The Stanford-SLAC CryoEM Center supplementU24GM129541 · NIGMS · STANFORD UNIVERSITY · PI CHIU, WAH, HEDMAN, BRITT · 2018 to 2023
$54.8M
NCCAT: National Center for CryoEM Access and Training- Supplement for Windows 10 and FFIU24GM129539 · NIGMS · NEW YORK STRUCTURAL BIOLOGY CENTER · PI DE MARCO, ALEX, KIEFT, JEFFREY S · 2018 to 2023
$53.9M
Structure and Function of AMPA subtype ionotropic glutamate receptorsR01NS083660 · NINDS · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI KURNIKOVA, MARIA G, SOBOLEVSKY, ALEXANDER · 2013 to 2022
$4.3M
Structure and function of Transient Receptor Potential ChannelsR01CA206573 · NCI · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI Alexander Sobolevsky · 2017 to 2026
$3.8M
Single-Particle Cryo-EM Characterization of AMPA Receptor Functional StatesR01NS107253 · NINDS · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI Alexander Sobolevsky · 2018 to 2026
$3.5M
NCI NIH HHS R01 CA206573NIGMS NIH HHS U24 GM129539NIGMS NIH HHS U24 GM129541NINDS NIH HHS R01 NS083660NINDS NIH HHS R01 NS107253
6 · The paper itself

Abstract

AMPA receptors (AMPARs) mediate the majority of excitatory neurotransmission. Their surface expression, trafficking, gating, and pharmacology are regulated by auxiliary subunits. Of the two types of TARP auxiliary subunits, type I TARPs assume activating roles, while type II TARPs serve suppressive functions. We present cryo-EM structures of GluA2 AMPAR in complex with type II TARP γ5, which reduces steady-state currents, increases single-channel conductance, and slows recovery from desensitization. Regulation of AMPAR function depends on its ligand-binding domain (LBD) interaction with the γ5 head domain. GluA2-γ5 complex shows maximum stoichiometry of two TARPs per AMPAR tetramer, being different from type I TARPs but reminiscent of the auxiliary subunit GSG1L. Desensitization of both GluA2-GSG1L and GluA2-γ5 complexes is accompanied by rupture of LBD dimer interface, while GluA2-γ5 but not GluA2-GSG1L LBD dimers remain two-fold symmetric. Different structural architectures and desensitization mechanisms of complexes with auxiliary subunits endow AMPARs with broad functional capabilities.

Indexed as

Amino Acid MotifsAnimalsCalcium ChannelsClaudinsCryoelectron MicroscopyDimerizationHEK293 CellsHumansImage Processing, Computer-AssistedLipid BilayersMembrane ProteinsMolecular ConformationPatch-Clamp TechniquesPolymersProtein BindingProtein ConformationCACNG5 protein, humanCacng5 protein, ratCalcium ChannelsClaudinsglutamate receptor ionotropic, AMPA 2GSG1L protein, humanGSG1L protein, ratLipid BilayersMembrane ProteinsPolymersReceptors, AMPAAMPA receptorcryo-EMcurrent kineticsdesensitizationgatingGSG1LiGluRsymmetryTARPγ5

Identifiers

PMID34678168
PMCPMC8642297

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Registered trials

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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 OpenQuestion graph.