A novel aspect of calpain activation

FEBS Letters

Sorimachi, Hiroyuki¹  Suzuki, Koichi¹ 

[1] Institute of Molecular and Cellular Biosciences, University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-0032, Japan

关键词: Calpain;    Protease;    Proteolysis;    Activation of calpain;    Ca2+;    Biomodulator;    CL;    calpain large subunit (80 kDa);    CS;    calpain small subunit (30 kDa);   

DOI  :  10.1016/S0014-5793(98)00856-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Calpain, a Ca²⁺-dependent biomodulator, alters the properties of substrate proteins by cleaving them at a limited number of specific sites. Recent studies of the structure-function relationship of calpain and X-ray analysis of its Ca²⁺-binding domain have revealed hitherto unknown features of the regulation of calpain activity. A novel dissociation/autolysis mechanism for the activation of calpain at the membrane is proposed, which incorporates recent findings from structure-function studies of calpain, and its implications are discussed.

【 授权许可】

Unknown