The Cl-/H+ antiporter ClC-7 is the primary chloride permeation pathway in lysosomes

Austin R. Graves, Patricia K. Curran, Carolyn L. Smith and Joseph A. Mindell ()
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Austin R. Graves: Membrane Transport Biophysics Unit, and,
Patricia K. Curran: Membrane Transport Biophysics Unit, and,
Carolyn L. Smith: Light Microscopy Facility, Porter Neuroscience Research Center, National Institute of Neurological Disorders and Stroke, National Institutes of Health, 35 Convent Drive, Building 35, MSC 3701, Bethesda, Maryland 20892, USA
Joseph A. Mindell: Membrane Transport Biophysics Unit, and,

Nature, 2008, vol. 453, issue 7196, 788-792

Abstract: Chloride permeation in lysosomes There has been much interest in the CLC family of membrane proteins since it has become apparent that some members are chlorine ion conducting ion channels whilst others are antiporters for chlorine and hydrogen ions. An antiporter is a membrane protein that is involved in active transport of two or more different ligands. In this paper, Graves et al. show that ClC-7 is a Cl−/H+ antiporter in lysosomal membranes, whose activity maintains the correct membrane voltage during acidification of the organelle. Interestingly, this work also reinforces the idea that plasma membrane CLCs are dedicated Cl− channels, whereas 'intracellular' CLCs are antiporters. This represents direct evidence that a CLC protein is responsible for the long-hypothesized chloride permeability of lysosomal membranes.

Date: 2008
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DOI: 10.1038/nature06907

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