Evidence map›Paper›PMID 24725410›Full record

ArticleCell2014

SWELL1, a plasma membrane protein, is an essential component of volume-regulated anion channel.

Zhaozhu Qiu, Adrienne E Dubin, Jayanti Mathur, Buu Tu, Kritika Reddy, Loren J Miraglia, Jürgen Reinhardt, Anthony P Orth, Ardem Patapoutian

Open access · bronzeAbstract read
In one paragraph

Article in Cell, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 366 papers.

0numbers the graph read from it
0cells of the map it votes in
366citing papers in PubMed
19.4field-weighted citation impact, top 1% 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

366 citing papers in PubMed, 569 citations in OpenAlex.

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors at 4 institutions in 2 countries.

Zhaozhu QiuGenomics Institute of the Novartis Research Foundation, San Diego, CA 92121, USA; Department of Molecular and Cellular Neuroscience, Howard Hughes Medical Institute, The Scripps Research Institute, La Jolla, CA 92037, USA.
Adrienne E DubinDepartment of Molecular and Cellular Neuroscience, Howard Hughes Medical Institute, The Scripps Research Institute, La Jolla, CA 92037, USA.
Jayanti MathurGenomics Institute of the Novartis Research Foundation, San Diego, CA 92121, USA.
Buu TuGenomics Institute of the Novartis Research Foundation, San Diego, CA 92121, USA.
Kritika ReddyGenomics Institute of the Novartis Research Foundation, San Diego, CA 92121, USA.
Loren J MiragliaGenomics Institute of the Novartis Research Foundation, San Diego, CA 92121, USA.
Jürgen ReinhardtNovartis Institutes for Biomedical Research, Basel 4056, Switzerland.
Anthony P OrthGenomics Institute of the Novartis Research Foundation, San Diego, CA 92121, USA.
Ardem PatapoutianDepartment of Molecular and Cellular Neuroscience, Howard Hughes Medical Institute, The Scripps Research Institute, La Jolla, CA 92037, USA. Electronic address: ardem@scripps.edu.
Genomics Institute of the Novartis Research Foundation · USHoward Hughes Medical Institute · USNovartis (Switzerland) · CHScripps Research Institute · US

Funding

Identification of novel somatosensory receptorsR01DE022115 · NIDCR · SCRIPPS RESEARCH INSTITUTE, THE · PI PATAPOUTIAN, ARDEM · 2011 to 2014
$1.5M
Howard Hughes Medical InstituteNIDCR NIH HHS R01 DE022115
6 · The paper itself

Abstract

Maintenance of a constant cell volume in response to extracellular or intracellular osmotic changes is critical for cellular homeostasis. Activation of a ubiquitous volume-regulated anion channel (VRAC) plays a key role in this process; however, its molecular identity in vertebrates remains unknown. Here, we used a cell-based fluorescence assay and performed a genome-wide RNAi screen to find components of VRAC. We identified SWELL1 (LRRC8A), a member of a four-transmembrane protein family with unknown function, as essential for hypotonicity-induced iodide influx. SWELL1 is localized to the plasma membrane, and its knockdown dramatically reduces endogenous VRAC currents and regulatory cell volume decrease in various cell types. Furthermore, point mutations in SWELL1 cause a significant change in VRAC anion selectivity, demonstrating that SWELL1 is an essential VRAC component. These findings enable further molecular characterization of the VRAC channel complex and genetic studies for understanding the function of VRAC in normal physiology and disease.

Indexed as

Cell SizeAnimalsCell MembraneGene Expression ProfilingGene Knockdown TechniquesGenome-Wide Association StudyHEK293 CellsHeLa CellsHumansIodidesMembrane ProteinsMiceRNA InterferenceIodidesLRRC8A protein, humanMembrane Proteins

Identifiers

PMID24725410
PMCPMC4023864
OpenAlexW2076968934

What OpenQuestion holds

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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.