Changes in intracellular calpastatin localization are mediated by reversible phosphorylation

被引：69

作者：

Averna, M ^{[1
]}

de Tullio, R ^{[1
]}

Passalacqua, M ^{[1
]}

Salamino, F ^{[1
]}

Pontremoli, S ^{[1
]}

Melloni, E ^{[1
]}

机构：

[1] Univ Genoa, Dept Expt Med, Biochem Sect, I-16132 Genoa, Italy

来源：

BIOCHEMICAL JOURNAL | 2001年 / 354卷

关键词：

calpain regulation; cAMP-dependent phosphorylation; LAN-5 neuroblastoma cells; phosphoprotein phosphatase;

D O I：

10.1042/0264-6021:3540025

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

We have previously reported that, in neuroblastoma LAN-5 cells, calpastatin is in an aggregated state, close to the cell nucleus [De Tullio, Passalacqua, Averna, Salamino, Melloni and Pontremoli (1999) Biochem. J, 343, 467-472]. In the present paper, we demonstrate that aggregated calpastatin is predominantly in a phosphorylated state. An increase in intracellular free [Ca2+] induces both dephosphorylation of calpastatin, through the action of a phosphoprotein phosphatase, and its redistribution as a soluble inhibitor species. cAMP, but not PMA- induced phosphorylation, reverses calpastatin distribution favouring its aggregation. This intracellular reversible mechanism, regulating the level of cytosolic calpastatin, could be considered a strategy through which calpain can escape calpastatin inhibition. especially during earlier steps of its activation process.

引用

页码：25 / 30

页数：6

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