Structural and functional characterization of the bestrophin-2 anion channel
نویسندگان
چکیده
منابع مشابه
Determinants of Anion Permeation in the Second Transmembrane Domain of the Mouse Bestrophin-2 Chloride Channel
Bestrophins have been proposed to constitute a new family of Cl channels that are activated by cytosolic Ca. We showed previously that mutation of serine-79 to cysteine in mouse bestrophin-2 (mBest2) altered the relative permeability and conductance to SCN. In this paper, we have overexpressed various mutant constructs of mBest2 in HEK-293 cells to explore the contributions to anion selectivity...
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15 صفحه اولMouse Bestrophin-2 Is a Bona fide Cl Channel: Identification of a Residue Important in Anion Binding and Conduction
Bestrophins have recently been proposed to comprise a new family of Cl channels. Our goal was to test whether mouse bestrophin-2 (mBest2) is a bona fide Cl channel. We expressed mBest2 in three different mammalian cell lines. mBest2 was trafficked to the plasma membrane as shown by biotinylation and immunoprecipitation, and induced a Ca 2 -activated Cl current in all three cell lines (EC 50 for...
متن کاملBestrophin-1 encodes for the Ca2+-activated anion channel in hippocampal astrocytes.
In mammalian brain, neurons and astrocytes are reported to express various chloride and anion channels, but the evidence for functional expression of Ca(2+)-activated anion channel (CAAC) and its molecular identity have been lacking. Here we report electrophysiological evidence for the CAAC expression and its molecular identity by mouse Bestrophin 1 (mBest1) in astrocytes of the mouse brain. Us...
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ژورنال
عنوان ژورنال: Nature Structural & Molecular Biology
سال: 2020
ISSN: 1545-9993,1545-9985
DOI: 10.1038/s41594-020-0402-z