Barttin Activates ClC-K Channel Function by Modulating Gating
نویسندگان
چکیده
منابع مشابه
Modulation of ClC-K channel function by the accessory subunit barttin.
The human ClC-Ka/ClC-Kb and rodent ClC-K1/ClC-K2 channels are the pore-forming channel proteins participating in electrolyte transport across the thick (ClC-Kb, ClC-K2) and thin (ClC-Ka, ClC-K1) ascending limbs of Henle’s Loop; further nephron segments, such as distal convoluted tubule and collecting duct (ClC-K2, ClC-Kb); and the marginal cells of the stria vascularis in the inner ear (ClC-Ka,...
متن کاملBarttin modulates trafficking and function of ClC-K channels.
Barttin is an accessory subunit of a subgroup of ClC-type chloride channels expressed in renal and inner ear epithelia. In this study, we examined the effects of barttin on two ClC-K channel isoforms, rat ClC-K1 and human ClC-Kb, using heterologous expression, patch clamping, confocal imaging, and flow cytometry. In the absence of barttin, only a small percentage of rClC-K1 and hClC-Kb channels...
متن کاملPhysiology and Pathophysiology of ClC-K/barttin Channels
ClC-K channels form a subgroup of anion channels within the ClC family of anion transport proteins. They are expressed predominantly in the kidney and in the inner ear, and are necessary for NaCl resorption in the loop of Henle and for K+ secretion by the stria vascularis. Subcellular distribution as well as the function of these channels are tightly regulated by an accessory subunit, barttin. ...
متن کاملReduced Membrane Insertion of CLC-K by V33L Barttin Results in Loss of Hearing, but Leaves Kidney Function Intact
In the mammalian ear, transduction of sound stimuli is initiated by K+ entry through mechano-sensitive channels into inner hair cells. K+ entry is driven by a positive endocochlear potential that is maintained by the marginal cell layer of the stria vascularis. This process requires basolateral K+ import by NKCC1 Na+-2Cl--K+ co-transporters as well as Cl- efflux through ClC-Ka/barttin or ClC-Kb...
متن کاملMolecular dissection of gating in the ClC-2 chloride channel.
The ClC-2 chloride channel is probably involved in the regulation of cell volume and of neuronal excitability. Site-directed mutagenesis was used to understand ClC-2 activation in response to cell swelling, hyperpolarization and acidic extracellular pH. Similar to equivalent mutations in ClC-0, neutralizing Lys566 at the end of the transmembrane domains results in outward rectification and a sh...
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ژورنال
عنوان ژورنال: Journal of the American Society of Nephrology
سال: 2010
ISSN: 1046-6673,1533-3450
DOI: 10.1681/asn.2009121274