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CLC chloride channels and transporters

Crystal structure of the bacterial CLC antiporter ClC-EC1 (Dutzler et al., Nature 2002)
Crystal structure of the bacterial CLC antiporter ClC-EC1 (Dutzler et al., Nature 2002)

I am interested in the biophysical characterization of the CLC protein family comprising chloride channels and chloride-coupled transporters and a better understanding of their physiological role.  The main focus is on two intracellular CLC antiporters, ClC-5 and ClC-7, expressed in endosomes and lysosomes, respectively. My laboratory mainly tackles these problems by electrophysiological techniques but I also combine them with spectroscopical approaches.

ClC-5 and ClC-7 are mutated in Dent disease and osteopetrosis, respectively, but their physiological role is far from clear and this problem is linked to a poor understanding of the role of chloride ions in intracellular organelles and, in general, of the mechanisms of ion transport and homeostasis in these compartments. I also work on developing new approaches to investigate these aspects.

Intracellular acidification

ClC-5 and ClC-7 are expressed in endosomes and lysosomes, respectively. It was thought for a long time that they provided a shunt conductance allowing vesicular acidification  mediated by  V-type ATPases. However, biophysical and physiological evidence suggest that their role is much more complex.

Our team

Selected publications

Related research themes