ArticlePloS one2012
Anion-sensitive fluorophore identifies the Drosophila swell-activated chloride channel in a genome-wide RNA interference screen.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 27 citations in OpenAlex.
- On the molecular nature of large-pore channels.Journal of molecular biology · 2021Review
- Glial Chloride Channels in the Function of the Nervous System Across Species.Advances in experimental medicine and biology · 2021Article
- Expression of LRRC8/VRAC Currents in Xenopus Oocytes: Advantages and Caveats.International journal of molecular sciences · 2018Review
- Molecular Biology and Physiology of Volume-Regulated Anion Channel (VRAC).Current topics in membranes · 2018Review
- Distribution and Function of the Bestrophin-1 (Best1) Channel in the Brain.Experimental neurobiology · 2017Review
- Bestrophin 1 and retinal disease.Progress in retinal and eye research · 2017Review
- Distinct regions that control ion selectivity and calcium-dependent activation in the bestrophin ion channel.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- VRACs and other ion channels and transporters in the regulation of cell volume and beyond.Nature reviews. Molecular cell biology · 2016Review
- Mitochondrial calcium uniporter regulator 1 (MCUR1) regulates the calcium threshold for the mitochondrial permeability transition.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Biophysics and Physiology of the Volume-Regulated Anion Channel (VRAC)/Volume-Sensitive Outwardly Rectifying Anion Channel (VSOR).Pflugers Archiv : European journal of physiology · 2016Review
- Bestrophin 1 is indispensable for volume regulation in human retinal pigment epithelium cells.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Bestrophin-1 influences transepithelial electrical properties and Ca2+ signaling in human retinal pigment epithelium.Molecular vision · 2015Article
- Article
- Hypotonicity stimulates potassium flux through the WNK-SPAK/OSR1 kinase cascade and the Ncc69 sodium-potassium-2-chloride cotransporter in the Drosophila renal tubule.The Journal of biological chemistry · 2014Article
- SWELL1, a plasma membrane protein, is an essential component of volume-regulated anion channel.Cell · 2014Article
- Deorphanizing the human transmembrane genome: A landscape of uncharacterized membrane proteins.Acta pharmacologica Sinica · 2014Review
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
When cells swell in hypo-osmotic solutions, chloride-selective ion channels (Cl(swell)) activate to reduce intracellular osmolality and prevent catastrophic cell rupture. Despite intensive efforts to assign a molecular identity to the mammalian Cl(swell) channel, it remains unknown. In an unbiased genome-wide RNA interference (RNAi) screen of Drosophila cells stably expressing an anion-sensitive fluorescent indicator, we identify Bestrophin 1 (dBest1) as the Drosophila Cl(swell) channel. Of the 23 screen hits with mammalian homologs and predicted transmembrane domains, only RNAi specifically targeting dBest1 eliminated the Cl(swell) current (I(Clswell)). We further demonstrate the essential contribution of dBest1 to Drosophila I(Clswell) with the introduction of a human Bestrophin disease-associated mutation (W94C). Overexpression of the W94C construct in Drosophila cells significantly reduced the endogenous I(Clswell). We confirm that exogenous expression of dBest1 alone in human embryonic kidney (HEK293) cells creates a clearly identifiable Drosophila-like I(Clswell). In contrast, activation of mouse Bestrophin 2 (mBest2), the closest mammalian ortholog of dBest1, is swell-insensitive. The first 64 residues of dBest1 conferred swell activation to mBest2. The chimera, however, maintains mBest2-like pore properties, strongly indicating that the Bestrophin protein forms the Cl(swell) channel itself rather than functioning as an essential auxiliary subunit. dBest1 is an anion channel clearly responsive to swell; this activation depends upon its N-terminus.
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Registered trials
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.