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凋亡过程中半胱天冬酶介导的PAK2激活:蛋白水解激酶激活作为凋亡信号转导的一般机制?

Caspase-mediated activation of PAK2 during apoptosis: proteolytic kinase activation as a general mechanism of apoptotic signal transduction?

作者信息

Bokoch G M

机构信息

Departments of Immunology and Cell Biology-IMM14, The Scripps Research Institute, 10550 N. Torrey Pines Road, La Jolla, CA 92037, USA.

出版信息

Cell Death Differ. 1998 Aug;5(8):637-45. doi: 10.1038/sj.cdd.4400405.

DOI:10.1038/sj.cdd.4400405
PMID:10200518
Abstract

p21-activated kinase 2 (PAK2) is proteolytically cleaved during apoptosis through the action of DEVD-sensitive caspase(s). This cleavage event causes PAK2 activation, and PAK2 activity is implicated in regulation of the biochemistry and morphology of the apoptotic cell. PAK2 is just one example of a number of identified caspase targets that are protein kinases involved in regulating various aspects of cell function. We hypothesize that this may reflect their important role in regulating the controlled and orderly demise of the dying cell.

摘要

p21激活激酶2(PAK2)在细胞凋亡过程中通过DEVD敏感的半胱天冬酶的作用被蛋白水解切割。这种切割事件导致PAK2激活,并且PAK2活性与凋亡细胞的生物化学和形态学调节有关。PAK2只是众多已确定的半胱天冬酶靶点之一,这些靶点是参与调节细胞功能各个方面的蛋白激酶。我们推测,这可能反映了它们在调节垂死细胞的可控和有序死亡中的重要作用。

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