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Summary
Calpain, an intracellular calcium-dependent protease, is activated at cell membranes and cleaves cytoskeletal and submembranous proteins. Calpain is inferred to be a calcium-dependent regulator for cytoskeletal reorganization. Calpastatin, an endogenous calpain inhibitor, inhibits not only the proteolytic activity of calpain but also the binding of calpain to membranes. Calpain activity is strictly regulated by calcium and calpastatin. Calpain has two distinct sites for interaction with calpastatin, one the active site and the other an EF-hand domain. It is believed that calpain interacts with substrates through the same two sites. We discuss the regulation of membrane binding and the activity of calpain through these two sites.
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