Evidence map›Paper›PMID 31615831›Full record

ReviewThe Journal of general physiology2019

Structural and functional insights into transmembrane AMPA receptor regulatory protein complexes.

Edward C Twomey, Maria V Yelshanskaya, Alexander I Sobolevsky

Open access · bronzeAbstract readReview
In one paragraph

Review in The Journal of general physiology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.4field-weighted citation impact, top 21% 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

25 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Temperature Sensitive Glutamate Gating of AMPA-subtype iGluRs.bioRxiv : the preprint server for biology · 2024
    Article
  12. Review
  13. Article
  14. Structure of Transmembrane AMPA Receptor Regulatory Protein Subunit γ2.bioRxiv : the preprint server for biology · 2023
    Article
  15. Article
  16. Article
  17. Article
  18. Small-animal PET study for noninvasive quantification of transmembrane AMPA receptor regulatory proteinJournal of cerebral blood flow and metabolism : official journal of the International Society of Cerebral Blood Flow and Metabolism · 2023
    Article
  19. Article
  20. Review
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

3 authors at 2 institutions in 1 country.

Edward C TwomeyDepartment of Cell Biology, Blavatnik Institute, Harvard Medical School, Boston, MA.ORCID 0000-0002-1855-1586
Maria V YelshanskayaDepartment of Biochemistry and Molecular Biophysics, Columbia University, New York, NY.
Alexander I SobolevskyDepartment of Biochemistry and Molecular Biophysics, Columbia University, New York, NY as4005@cumc.columbia.edu.ORCID 0000-0001-5181-8644
Columbia University · USHarvard University · US

Funding

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 CA206573NINDS NIH HHS R01 NS083660NINDS NIH HHS R01 NS107253
6 · The paper itself

Abstract

Fast excitatory neurotransmission is mediated by the α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) subtype of ionotropic glutamate receptor (AMPAR). AMPARs initiate depolarization of the postsynaptic neuron by allowing cations to enter through their ion channel pores in response to binding of the neurotransmitter glutamate. AMPAR function is dramatically affected by auxiliary subunits, which are regulatory proteins that form various complexes with AMPARs throughout the brain. The most well-studied auxiliary subunits are the transmembrane AMPAR regulatory proteins (TARPs), which alter the assembly, trafficking, localization, kinetics, and pharmacology of AMPARs. Recent structural and functional studies of TARPs and the TARP-fold germ cell-specific gene 1-like (GSG1L) subunit have provided important glimpses into how auxiliary subunits regulate the function of synaptic complexes. In this review, we put these recent structures in the context of new functional findings in order to gain insight into the determinants of AMPAR regulation by TARPs. We thus reveal why TARPs display a broad range of effects despite their conserved modular architecture.

Indexed as

AnimalsBrainClaudinsGlutamic AcidHumansMembrane ProteinsNeuronsProtein TransportReceptors, AMPASynaptic TransmissionClaudinsGlutamic AcidMembrane ProteinsReceptors, AMPA

Identifiers

PMID31615831
PMCPMC6888759
OpenAlexW2981043760

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.