Evidence map›Paper›PMID 32012213›Full record

ArticleThe Journal of general physiology2020

Insights into the molecular mechanisms underlying the inhibition of acid-sensing ion channel 3 gating by stomatin.

Robert C Klipp, Megan M Cullinan, John R Bankston

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of general physiology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.5field-weighted citation impact, top 10% 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

21 citing papers in PubMed, 39 citations in OpenAlex.

  1. Article
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  4. Progress on functions of intracellular domainZhejiang da xue xue bao. Yi xue ban = Journal of Zhejiang University. Medical sciences · 2024
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  19. Acid-Sensing Ion Channels and Mechanosensation.International journal of molecular sciences · 2021
    Review
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Robert C Klipp
Megan M CullinanDepartment of Physiology and Biophysics, University of Colorado Anschutz Medical Campus, School of Medicine, Aurora, CO.
John R BankstonDepartment of Physiology and Biophysics, University of Colorado Anschutz Medical Campus, School of Medicine, Aurora, CO.
University of Colorado Anschutz Medical Campus · US

Funding

POSTGRADUATE TRAINING IN CARDIOVASCULAR RESEARCHT32HL007822 · NHLBI · UNIVERSITY OF COLORADO DENVER · PI BUTTRICK, PETER N., LEINWAND, LESLIE ANNE · 1996 to 2023
$6.2M
Function and regulation of acid-sensing ion channels in corneal neuronsR00EY024267 · NEI · UNIVERSITY OF COLORADO DENVER · PI BANKSTON, JOHN · 2017 to 2019
$747k
Structural Mechanisms of Acid Sensing Ion ChannelsF31DE028739 · NIDCR · UNIVERSITY OF COLORADO DENVER · PI CULLINAN, MEGAN · 2019 to 2021
$105k
NEI NIH HHS R00 EY024267NHLBI NIH HHS T32 HL007822NIDCR NIH HHS F31 DE028739
6 · The paper itself

Abstract

Stomatin (STOM) is a monotopic integral membrane protein found in all classes of life that has been shown to regulate members of the acid-sensing ion channel (ASIC) family. However, the mechanism by which STOM alters ASIC function is not known. Using chimeric channels, we combined patch-clamp electrophysiology and FRET to search for regions of ASIC3 critical for binding to and regulation by STOM. With this approach, we found that regulation requires two distinct sites on ASIC3: the distal C-terminus and the first transmembrane domain (TM1). The C-terminal site is critical for formation of the STOM-ASIC3 complex, while TM1 is required only for the regulatory effect. We then looked at the mechanism of STOM-dependent regulation of ASIC3 and found that STOM does not alter surface expression of ASIC3 or shift the pH dependence of channel activation. However, a point mutation (Q269G) that prevents channel desensitization also prevents STOM regulation, suggesting that STOM may alter ASIC3 currents by stabilizing the desensitized state of the channel. Based on these findings, we propose a model whereby STOM is anchored to the channel via a site on the distal C-terminus and stabilizes the desensitized state of the channel via an interaction with TM1.

Indexed as

Acid Sensing Ion ChannelsAnimalsCell LineCHO CellsCricetulusElectrophysiologyHydrogen-Ion ConcentrationIon Channel GatingMembrane ProteinsNeuronsProtein DomainsRatsAcid Sensing Ion ChannelsASIC3 protein, ratMembrane ProteinsStom protein, rat

Identifiers

PMID32012213
PMCPMC7054857
OpenAlexW3005437014

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.