ClC-1 is a Cl- channel in mammalian skeletal muscle that plays an important role in membrane repolarization following muscular contraction. Reduction of ClC-1 conductance results in myotonia, a state characterized by muscle hyperexcitability. As is the case for other members of the ClC family, ClC-1 exists as a dimer that forms a double-barrelled channel. Each barrel, or pore, of ClC-1 is gated by its own gate ('fast' or 'single pore' gate), whereas both pores are gated simultaneously by another mechanism ('slow' or 'common' gate).

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Comparison of the biophysical and pharmacological properties of heterologously expressed ClC-1 with the properties of the Cl- conductance measured in skeletal muscle strongly suggests that ClC-1 is the major Cl- channel responsible for muscle repolarization. However, not all results obtained in experiments on whole muscle or muscle fibres support this notion. In the present review we attempt to bring together the current knowledge of ClC-1 with the physiology of skeletal muscle.