Barttin increases surface expression and changes current properties of ClC-K channels. Conservation of chloride channel structure revealed by an inhibitor binding site in ClC-1. Fast and slow gating relaxations in the muscle chloride channel CLC-1. Pore-forming segments in voltage-gated chloride channels. Characterization of the mouse ClC-K1/Barttin chloride channel. Functional and structural analysis of ClC-K chloride channels involved in renal disease. Barttin modulates trafficking and function of ClC-K channels. Barttin is a Cl − channel β-subunit crucial for renal Cl − reabsorption and inner ear K + secretion. Two highly homologous members of the ClC chloride channel family in both rat and human kidney. Kieferle, S., Fong, P., Bens, M., Vandewalle, A. Two isoforms of a chloride channel predominantly expressed in thick ascending limb of Henle’s loop and collecting ducts of rat kidney. Structure of a eukaryotic CLC transporter defines an intermediate state in the transport cycle. Gating the selectivity filter in ClC chloride channels. X-ray structure of a ClC chloride channel at 3.0 Å reveals the molecular basis of anion selectivity. Two physically distinct pores in the dimeric ClC-0 chloride channel. Ion permeation through a Cl −-selective channel designed from a CLC Cl −/H + exchanger. Jayaram, H., Accardi, A., Wu, F., Williams, C. ![]() Uncoupling and turnover in a Cl −/H + exchange transporter. Chloride/proton antiporter activity of mammalian CLC proteins ClC-4 and ClC-5. Voltage-dependent electrogenic chloride/proton exchange by endosomal CLC proteins. Secondary active transport mediated by a prokaryotic homologue of ClC Cl − channels. Primary structure of Torpedo marmorata chloride channel isolated by expression cloning in Xenopus oocytes. Dimeric structure of single chloride channels from Torpedo electroplax. Loss of the ClC-7 chloride channel leads to osteopetrosis in mice and man. Isolation and partial characterization of a chloride channel gene which is expressed in kidney and is a candidate for Dent’s disease (an X-linked hereditary nephrolithiasis). Mutations in the chloride channel gene, CLCNKB, cause Bartter’s syndrome type III. The skeletal muscle chloride channel in dominant and recessive human myotonia. ClC chloride channels viewed through a transporter lens. A decade of CLC chloride channels: structure, mechanism, and many unsettled questions. Discovery of CLC transport proteins: cloning, structure, function and pathophysiology. Thus, reduction of a kinetic barrier in CLC channels enables fast flow of Cl − down its electrochemical gradient. Consequently, the cytosolic constriction for Cl − passage is widened in CLC-K such that the kinetic barrier previously postulated for Cl −/H + transporter function would be reduced. A conserved loop in the Cl − transport pathway shows a structure markedly different from that of CLC transporters. Here we determined the structure of a bovine CLC channel (CLC-K) using cryo-electron microscopy. ![]() The structural basis underlying these distinctive transport mechanisms is puzzling because CLC channels and transporters are expected to share the same architecture on the basis of sequence homology. Some CLC proteins are channels that conduct Cl − ions passively, whereas others are secondary active transporters that exchange two Cl − ions for one H +. CLC proteins transport chloride (Cl −) ions across cellular membranes to regulate muscle excitability, electrolyte movement across epithelia, and acidification of intracellular organelles.
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