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Article

Suppressed disassembly of autolyzing p94/CAPN3 by N2A connectin/titin in a genetic reporter system.

The Journal of biological chemistry - 7 Jul 2006

Ono Yasuko, Torii Fukuyo, Ojima Koichi, Doi Naoko, Yoshioka Katsuhide, Kawabata Yukiko, Labeit Dietmar, Labeit Siegfried, Suzuki Koichi, Abe Keiko, Maeda Tatsuya, Sorimachi Hiroyuki

Abstract excerpt

p94/calpain 3 is a skeletal muscle-specific member of the Ca(2+)-regulated cytosolic cysteine protease family, the calpains. Defective p94 protease activity originating from gene mutations causes a muscular dystrophy called calpainopathy, indicating the indispensability of p94 for muscle survival. Because of the existence of the p94-specific regions IS1 and IS2, p94 undergoes very rapid and exhaustive autolysis....

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Identifiers

PMID: 16627476
DOI: 10.1074/jbc.M601029200

Genes

CAPN3

Variants

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Suppressed disassembly of autolyzing p94/CAPN3 by N2A connectin/titin in a genetic reporter system.PMID 16627476Read ↗

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An eccentric calpain, CAPN3/p94/calpain-3.Semantic proximity Read ↗

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The N- and C-terminal autolytic fragments of CAPN3/p94/calpain-3 restore proteolytic activity by intermolecular complementation.Semantic proximity Read ↗

Skeletal muscle-specific calpain is an intracellular Na+-dependent protease.Semantic proximity Read ↗

Dynamic distribution of muscle-specific calpain in mice has a key role in physical-stress adaptation and is impaired in muscular dystrophySemantic proximity Read ↗

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Oligomer-dependent and oligomer-independent pathogenesis of muscular dystrophy-associated mutations within the penta-EF-hand domain of calpain-3.Semantic proximity Read ↗

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