Evidence map›Paper›PMID 22813734›Full record

ArticleCell reports2012

Differences in AMPA and kainate receptor interactomes facilitate identification of AMPA receptor auxiliary subunit GSG1L.

Natalie F Shanks, Jeffrey N Savas, Tomohiko Maruo, Ondrej Cais, Atsushi Hirao, Souichi Oe, Anirvan Ghosh, Yasuko Noda, Ingo H Greger, John R Yates and 1 more

Open access · goldAbstract read
In one paragraph

Article in Cell reports, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 124 papers.

0numbers the graph read from it
0cells of the map it votes in
124citing papers in PubMed
5.4field-weighted citation impact, top 3% 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

124 citing papers in PubMed, 187 citations in OpenAlex.

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64 more citing papers are in PubMed but not listed here.

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

11 authors at 4 institutions in 3 countries.

Natalie F ShanksDepartment of Chemistry and Biochemistry, University of California, San Diego, La Jolla, CA 92093, USA.
Jeffrey N Savas
Tomohiko Maruo
Ondrej Cais
Atsushi Hirao
Souichi Oe
Anirvan Ghosh
Yasuko Noda
Ingo H Greger
John R Yates
Terunaga Nakagawa
University of California, San Diego · USJichi Medical University · JPMRC Laboratory of Molecular Biology · GBScripps Research Institute · US

Funding

ZDS2P REGULATES SWE1P-DEPENDENT POLARIZED CELL GROWTH IN S CEREVISIAEP41RR011823 · NCRR · UNIVERSITY OF WASHINGTON · PI DAVIS, TRACY · 1996 to 2011
$24.7M
TrainingP41GM103533 · NIGMS · UNIVERSITY OF WASHINGTON · PI MACCOSS, MICHAEL · 2012 to 2021
$20.7M
Neurosciences Graduate Training ProgramT32NS061847 · NINDS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI Brenda L Bloodgood · 2008 to 2026
$7.7M
Quantitative Proteome Analysis of Brain DevelopmentR01MH067880 · NIMH · SCRIPPS RESEARCH INSTITUTE, THE · PI YATES III, JOHN R · 2003 to 2017
$7.1M
Molecular Anatomy of Mature and Immature Glutamate ReceptorsR01HD061543 · NICHD · VANDERBILT UNIVERSITY · PI NAKAGAWA, TERUNAGA · 2010 to 2014
$1.5M
Quantitative Proteomic Approach to Identify the Mechanism of Alzheimer's DiseaseF32AG039127 · NIA · SCRIPPS RESEARCH INSTITUTE, THE · PI SAVAS, JEFFREY NICHOLAS · 2011 to 2014
$117k
Medical Research Council MC_U105174197NCRR NIH HHS P41 RR011823NIA NIH HHS 1F32AG039127NIA NIH HHS F32 AG039127NICHD NIH HHS R01 HD061543NIGMS NIH HHS P41 GM103533NIMH NIH HHS R01 MH067880NINDS NIH HHS T32 NS061847
6 · The paper itself

Abstract

AMPA receptor (AMPA-R) complexes consist of channel-forming subunits, GluA1-4, and auxiliary proteins, including TARPs, CNIHs, synDIG1, and CKAMP44, which can modulate AMPA-R function in specific ways. The combinatorial effects of four GluA subunits binding to various auxiliary subunits amplify the functional diversity of AMPA-Rs. The significance and magnitude of molecular diversity, however, remain elusive. To gain insight into the molecular complexity of AMPA and kainate receptors, we compared the proteins that copurify with each receptor type in the rat brain. This interactome study identified the majority of known interacting proteins and, more importantly, provides candidates for additional studies. We validate the claudin homolog GSG1L as a newly identified binding protein and unique modulator of AMPA-R gating, as determined by detailed molecular, cellular, electrophysiological, and biochemical experiments. GSG1L extends the functional variety of AMPA-R complexes, and further investigation of other candidates may reveal additional complexity of ionotropic glutamate receptor function.

Indexed as

Protein Interaction MapsAmino Acid SequenceAnimalsBrainClaudinsHEK293 CellsHumansKainic Acid ReceptorsMaleMass SpectrometryMembrane ProteinsMolecular Sequence DataNeuronsProtein BindingProteinsProtein SubunitsClaudinsGSG1L protein, ratKainic Acid ReceptorsMembrane ProteinsProteinsProtein SubunitsReceptors, AMPA

Identifiers

PMID22813734
PMCPMC3401968
OpenAlexW2129843185

What OpenQuestion holds

Textmetadata
LicenceTDM
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.