Evidence map›Paper›PMID 24790029›Full record

ArticleScience (New York, N.Y.)2014

Identification of LRRC8 heteromers as an essential component of the volume-regulated anion channel VRAC.

Felizia K Voss, Florian Ullrich, Jonas Münch, Katina Lazarow, Darius Lutter, Nancy Mah, Miguel A Andrade-Navarro, Jens P von Kries, Tobias Stauber, Thomas J Jentsch

Abstract read
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In one paragraph

Article in Science (New York, N.Y.), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 376 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
376citing papers in PubMed, 1 pooled it
21.1field-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

376 citing papers in PubMed, 1 synthesis or guideline pooled it, 629 citations in OpenAlex.

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  16. Mechanosensitive ion channels as novel targets in osteoporosis.Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research · 2026
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316 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

10 authors at 1 institution in 1 country.

Felizia K VossLeibniz-Institut für Molekulare Pharmakologie (FMP), Berlin.
Florian Ullrich
Jonas Münch
Katina Lazarow
Darius Lutter
Nancy Mah
Miguel A Andrade-Navarro
Jens P von Kries
Tobias Stauber
Thomas J Jentsch
Max Delbrück Center · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Regulation of cell volume is critical for many cellular and organismal functions, yet the molecular identity of a key player, the volume-regulated anion channel VRAC, has remained unknown. A genome-wide small interfering RNA screen in mammalian cells identified LRRC8A as a VRAC component. LRRC8A formed heteromers with other LRRC8 multispan membrane proteins. Genomic disruption of LRRC8A ablated VRAC currents. Cells with disruption of all five LRRC8 genes required LRRC8A cotransfection with other LRRC8 isoforms to reconstitute VRAC currents. The isoform combination determined VRAC inactivation kinetics. Taurine flux and regulatory volume decrease also depended on LRRC8 proteins. Our work shows that VRAC defines a class of anion channels, suggests that VRAC is identical to the volume-sensitive organic osmolyte/anion channel VSOAC, and explains the heterogeneity of native VRAC currents.

Indexed as

Cell SizeAgammaglobulinemiaChloride ChannelsGene Knockout TechniquesGenome-Wide Association StudyHCT116 CellsHEK293 CellsHumansMembrane ProteinsMutationProtein MultimerizationRNA InterferenceRNA, Small InterferingTaurineTransfectionChloride ChannelsLRRC8A protein, humanMembrane ProteinsRNA, Small InterferingTaurine

Identifiers

PMID24790029
OpenAlexW2046464107

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.