Evidence map›Paper›PMID 17898214›Full record

ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2007

Critical roles for the M3-S2 transduction linker domain in kainate receptor assembly and postassembly trafficking.

Pornpun Vivithanaporn, Laura Leanne Lash, William Marszalec, Geoffrey T Swanson

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
0.9field-weighted citation impact, top 29% 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

18 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
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  6. Review
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  10. Review
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  12. Synaptic targeting and functional modulation of GluK1 kainate receptors by the auxiliary neuropilin and tolloid-like (NETO) proteins.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2011
    Article
  13. Article
  14. Article
  15. Ion-dependent gating of kainate receptors.The Journal of physiology · 2010
    Review
  16. Article
  17. Article
  18. 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

4 authors at 1 institution in 1 country.

Pornpun VivithanapornDepartment of Pharmacology and Toxicology, University of Texas Medical Branch, Galveston, Texas 77555, USA.
Laura Leanne Lash
William Marszalec
Geoffrey T Swanson
Northwestern University · US

Funding

RXR motifs as ER retention signals in kainate receptorsR03MH065289 · NIMH · UNIVERSITY OF TEXAS MEDICAL BR GALVESTON · PI SWANSON, GEOFFREY T · 2002 to 2003
$149k
NIMH NIH HHS R03 MH65289
6 · The paper itself

Abstract

Kainate receptors (KARs) are neuronal proteins that exhibit a highly polarized distribution in the mammalian CNS. Assembly, intracellular trafficking, and synaptic targeting of KARs and other ionotropic glutamate receptors are processes controlled, in part, by various determinants within the constituent subunit proteins themselves. Here, we demonstrate that the linker region between the M3 and S2 domains, which in current structural models is thought to transduce ligand-binding energy into channel opening, additionally has an essential role in receptor biogenesis. Our results show that this gating-associated domain is engaged at two distinct critical stages of KAR biogenesis: first, during the transition from dimeric to tetrameric assembly states and, second, at a postassembly trafficking checkpoint within the endoplasmic reticulum. Alteration of a basic residue, arginine 663, altered the desensitization properties of the GluR6 kainate receptor in response to glutamate application, and these changes were weakly correlated with intracellular retention of the mutant receptors. Elimination of the positive charge also significantly attenuated oligomerization and stability of the intracellular subunit protein. Furthermore, charge swapping with an adjacent residue, glutamate 662, normalized the receptor physiological behavior and reversed the deficits in assembly and degradation, but only partially restored plasma membrane expression of the receptors. These results reveal a new role for this linker domain in glutamate receptor biogenesis and contribute to understanding the cellular controls of receptor assembly and trafficking, which will be important for relating receptor stoichiometry to their neuronal targeting and function.

Indexed as

AnimalsCell MembraneGluK2 Kainate ReceptorHippocampusKainic Acid ReceptorsMutationNeuronsProtein Structure, TertiaryProtein TransportRatsRats, Sprague-DawleyGluK2 Kainate ReceptorKainic Acid Receptors

Identifiers

PMID17898214
PMCPMC6673142
OpenAlexW2168658666

What OpenQuestion holds

Textmetadata
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.