Evidence map›Paper›PMID 25422502›Full record

ArticleThe Journal of general physiology2014

Stargazin promotes closure of the AMPA receptor ligand-binding domain.

David M MacLean, Swarna S Ramaswamy, Mei Du, James R Howe, Vasanthi Jayaraman

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of general physiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
3.0field-weighted citation impact, top 9% of its field
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

36 citing papers in PubMed, 47 citations in OpenAlex.

  1. Article
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  3. Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Activity Dependent Inhibition of AMPA Receptors by ZnThe Journal of neuroscience : the official journal of the Society for Neuroscience · 2020
    Article
  10. Article
  11. Conformational spread and dynamics in allostery of NMDA receptors.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  12. Mechanism of modulation of AMPA receptors by TARP-γ8.The Journal of general physiology · 2020
    Article
  13. Article
  14. Review
  15. Article
  16. Review
  17. Single-Molecule FRET Methods to Study Glutamate Receptors.Methods in molecular biology (Clifton, N.J.) · 2019
    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 at 1 institution in 1 country.

David M MacLeanDepartment of Biochemistry and Molecular Biology, Center for Membrane Biology, University of Texas Health Science Center, Houston, TX 77030.
Swarna S RamaswamyDepartment of Biochemistry and Molecular Biology, Center for Membrane Biology, University of Texas Health Science Center, Houston, TX 77030.
Mei DuDepartment of Biochemistry and Molecular Biology, Center for Membrane Biology, University of Texas Health Science Center, Houston, TX 77030.
James R HoweDepartment of Pharmacology, Yale University School of Medicine, New Haven, CT 06530.
Vasanthi JayaramanDepartment of Biochemistry and Molecular Biology, Center for Membrane Biology, University of Texas Health Science Center, Houston, TX 77030 vasanthi.jayaraman@uth.tmc.edu.
Yale University · US

Funding

Structure and Function of NMDA ReceptorsR01GM094246 · NIGMS · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI JAYARAMAN, VASANTHI · 2011 to 2016
$2.0M
NIGMS NIH HHS GM094246NIGMS NIH HHS R01 GM094246
6 · The paper itself

Abstract

Transmembrane AMPA receptor (AMPAR) regulatory proteins (TARPs) markedly enhance AMPAR function, altering ligand efficacy and receptor gating kinetics and thereby shaping the postsynaptic response. The structural mechanism underlying TARP effects on gating, however, is unknown. Here we find that the prototypical member of the TARP family, stargazin or γ-2, rescues gating deficits in AMPARs carrying mutations that destabilize the closed-cleft states of the ligand-binding domain (LBD), suggesting that stargazin reverses the effects of these mutations and likely stabilizes closed LBD states. Furthermore, stargazin promotes a more closed conformation of the LBD, as indicated by reduced accessibility to the large antagonist NBQX. Consistent with the functional studies, luminescence resonance energy transfer experiments directly demonstrate that the AMPAR LBD is on average more closed in the presence of stargazin, in both the apo and agonist-bound states. The additional cleft closure and/or stabilization of the more closed-cleft states of the LBD is expected to translate to higher agonist efficacy and could contribute to the structural mechanism for stargazin modulation of AMPAR function.

Indexed as

Calcium ChannelsCell Membrane PermeabilityHEK293 CellsHumansIon Channel GatingLigandsProtein BindingProtein ConformationProtein Structure, TertiaryReceptors, AMPACACNG2 protein, humanCalcium ChannelsLigandsReceptors, AMPA

Identifiers

PMID25422502
PMCPMC4242809
OpenAlexW1979045753

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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 OpenQuestion graph.