ArticleThe Journal of general physiology2008
Rescue of volume-regulated anion current by bestrophin mutants with altered charge selectivity.
Article in The Journal of general physiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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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.
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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.
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Who cites it
19 citing papers in PubMed, 33 citations in OpenAlex.
- Interaction with stomatin directs human proton channels into cholesterol-dependent membrane domains.Biophysical journal · 2024Article
- Glial Chloride Channels in the Function of the Nervous System Across Species.Advances in experimental medicine and biology · 2021Article
- Sensing through Non-Sensing Ocular Ion Channels.International journal of molecular sciences · 2020Review
- 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
- 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
- Article
- Structure and selectivity in bestrophin ion channels.Science (New York, N.Y.) · 2014Article
- 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
- Drosophila bestrophin-1 currents are regulated by phosphorylation via a CaMKII dependent mechanism.PloS one · 2013Article
- Anion-sensitive fluorophore identifies the Drosophila swell-activated chloride channel in a genome-wide RNA interference screen.PloS one · 2012Article
- Calcium-activated chloride current expression in axotomized sensory neurons: what for?Frontiers in molecular neuroscience · 2012Article
- Bestrophins and retinopathies.Pflugers Archiv : European journal of physiology · 2010Review
- Chloride channels: often enigmatic, rarely predictable.Annual review of physiology · 2010Review
- Dysregulation of human bestrophin-1 by ceramide-induced dephosphorylation.The Journal of physiology · 2009Article
- Bestrophin expression and function in the human pancreatic duct cell line, CFPAC-1.The Journal of physiology · 2009Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Mutations in human bestrophin-1 are linked to various kinds of retinal degeneration. Although it has been proposed that bestrophins are Ca(2+)-activated Cl(-) channels, definitive proof is lacking partly because mice with the bestrophin-1 gene deleted have normal Ca(2+)-activated Cl(-) currents. Here, we provide compelling evidence to support the idea that bestrophin-1 is the pore-forming subunit of a cell volume-regulated anion channel (VRAC) in Drosophila S2 cells. VRAC was abolished by treatment with RNAi to Drosophila bestrophin-1. VRAC was rescued by overexpressing bestrophin-1 mutants with altered biophysical properties and responsiveness to sulfhydryl reagents. In particular, the ionic selectivity of the F81C mutant changed from anionic to cationic when the channel was treated with the sulfhydryl reagent, sodium (2-sulfonatoethyl) methanethiosulfonate (MTSES(-)) (P(Cs)/P(Cl) = 0.25 for native and 2.38 for F81C). The F81E mutant was 1.3 times more permeable to Cs(+) than Cl(-). The finding that VRAC was rescued by F81C and F81E mutants with different biophysical properties shows that bestrophin-1 is a VRAC in S2 cells and not simply a regulator or an auxiliary subunit. F81C overexpressed in HEK293 cells also exhibits a shift of ionic selectivity after MTSES(-) treatment, although the effect is quantitatively smaller than in S2 cells. To test whether bestrophins are VRACs in mammalian cells, we compared VRACs in peritoneal macrophages from wild-type mice and mice with both bestrophin-1 and bestrophin-2 disrupted (best1(-/-)/best2(-/-)). VRACs were identical in wild-type and best1(-/-)/best2(-/-) mice, showing that bestrophins are unlikely to be the classical VRAC in mammalian cells.
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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.