Proteolytic activation of MST/Krs, STE20-related protein kinase, by caspase during apoptosis

被引：120

作者：

Lee, KK

Murakawa, M

Nishida, E

Tsubuki, S

Kawashima, S

Sakamaki, K

Yonehara, S ^{[1
]}

机构：

[1] Kyoto Univ, Inst Virus Res, Kyoto 60601, Japan

[2] Tokyo Metropolitan Inst Med Sci, Tokyo 113, Japan

[3] Kyoto Univ, Fac Sci, Dept Biophys, Kyoto 60601, Japan

来源：

ONCOGENE | 1998年 / 16卷 / 23期

关键词：

Fas (Apo-1/CD95); apoptosis; caspase; protein kinase; signal transduction;

D O I：

10.1038/sj.onc.1201840

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：

The Fas system has been extensively investigated as a model of apoptosis and the caspase cascade has been shown to be a characteristic mechanism of signaling of apoptosis. We have identified and purified a kinase that was activated after the stimulation of Fas on human thymoma-derived HPB-ALL cells. Partial amino acid sequencing of the purified kinase revealed it to be MST/ Krs, member of the yeast STE20 family of protein kinases. MST/Krs was activated by proteolytic cleavage and proteolytic activation was blocked by the caspase inhibitor, Z-VAD-FK. A mutant MST with Asp-->Asn replacement at a putative caspase cleavage site was resistant to either the proteolytic cleavage or the activation of the kinase activity. These findings suggest that proteolytic activation is one activation mechanism of MST and plays a role in apoptosis.

引用

收藏

页码：3029 / 3037

页数：9

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