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Physiological Reviews, Vol. 82, No. 2, April 2002, pp. 503-568; 10.1152/physrev.00029.2001.
Copyright ©2002 by the American Physiological Society
Zentrum für Molekulare Neurobiologie Hamburg, Universität Hamburg, Hamburg, Germany
Jentsch, Thomas J.,
Valentin Stein,
Frank Weinreich, and
Anselm A. Zdebik.
Molecular Structure and Physiological Function of Chloride
Channels. Physiol. Rev. 82: 503-568, 2002.
Cl
channels reside both in
the plasma membrane and in intracellular organelles. Their functions
range from ion homeostasis to cell volume regulation, transepithelial
transport, and regulation of electrical excitability. Their
physiological roles are impressively illustrated by various inherited
diseases and knock-out mouse models. Thus the loss of distinct
Cl channels leads to an impairment of transepithelial
transport in cystic fibrosis and Bartter's syndrome, to increased
muscle excitability in myotonia congenita, to reduced endosomal
acidification and impaired endocytosis in Dent's disease, and to
impaired extracellular acidification by osteoclasts and osteopetrosis.
The disruption of several Cl channels in mice results in
blindness. Several classes of Cl channels have not yet
been identified at the molecular level. Three molecularly distinct
Cl channel families (CLC, CFTR, and ligand-gated GABA
and glycine receptors) are well established. Mutagenesis and functional
studies have yielded considerable insights into their structure and
function. Recently, the detailed structure of bacterial CLC proteins
was determined by X-ray analysis of three-dimensional crystals.
Nonetheless, they are less well understood than cation channels and
show remarkably different biophysical and structural properties. Other
gene families (CLIC or CLCA) were also reported to encode
Cl channels but are less well characterized. This review
focuses on molecularly identified Cl channels and their
physiological roles.
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