Direct endosomal acidification by the outwardly rectifying CLC‐5 Cl − /H + exchanger
نویسندگان
چکیده
منابع مشابه
Criteria for the Molecular Identification of the Volume-Sensitive Outwardly Rectifying Cl− Channel
Anion channels are activated by volume expansion in most animal cell types and are known to be implicated not only in regulatory volume decrease but also in many other cell activities that are associated with changes in cell volume and shape, including cell proliferation and cell death (Okada, 1998). Among a variety of swellingactivated Cl 2 channels (I Cl.swell ), the most important and freque...
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TMEM16 (transmembrane protein 16) proteins, which possess eight putative transmembrane domains with intracellular NH2- and COOH-terminal tails, are thought to comprise a Cl(-) channel family. The function of TMEM16F, a member of the TMEM16 family, has been greatly controversial. In the present study, we performed whole cell patch-clamp recordings to investigate the function of human TMEM16F. In...
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To facilitate polarized vesicular trafficking and signal transduction, neuronal endosomes have evolved sophisticated mechanisms for pH homeostasis. NHE5 is a member of the Na(+)/H(+) exchanger family and is abundantly expressed in neurons and associates with recycling endosomes. Here we show that NHE5 potently acidifies recycling endosomes in PC12 cells. NHE5 depletion by plasmid-based short ha...
متن کاملProton block of the CLC-5 Cl−/H+ exchanger
CLC-5 is a H(+)/Cl(-) exchanger that is expressed primarily in endosomes but can traffic to the plasma membrane in overexpression systems. Mutations altering the expression or function of CLC-5 lead to Dent's disease. Currents mediated by this transporter show extreme outward rectification and are inhibited by acidic extracellular pH. The mechanistic origins of both phenomena are currently not ...
متن کاملSeparate Ion Pathways in a Cl−/H+ Exchanger
CLC-ec1 is a prokaryotic CLC-type Cl(-)/H+ exchange transporter. Little is known about the mechanism of H+ coupling to Cl-. A critical glutamate residue, E148, was previously shown to be required for Cl(-)/H+ exchange by mediating proton transfer between the protein and the extracellular solution. To test whether an analogous H+ acceptor exists near the intracellular side of the protein, we per...
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ژورنال
عنوان ژورنال: The Journal of Physiology
سال: 2010
ISSN: 0022-3751,1469-7793
DOI: 10.1113/jphysiol.2010.188540