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Thus the loss of distinct Cl<jats:sup>\u2212<\/jats:sup>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<jats:sup>\u2212<\/jats:sup>channels in mice results in blindness. Several classes of Cl<jats:sup>\u2212<\/jats:sup>channels have not yet been identified at the molecular level. Three molecularly distinct Cl<jats:sup>\u2212<\/jats:sup>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<jats:sup>\u2212<\/jats:sup>channels but are less well characterized. 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