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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Activation of hPAK65 by caspase cleavage induces some of the morphological and biochemical changes of apoptosis
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Activation of hPAK65 by caspase cleavage induces some of the morphological and biochemical changes of apoptosis

机译:半胱天冬酶裂解激活hPAK65诱导细胞凋亡的一些形态和生化变化

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摘要

Apoptosis is a highly regulated form of cell death, characterized by distinctive features such as cellular shrinkage and nuclear condensation. We demonstrate here that proteolytic activation of hPAK65, a p21-activated kinase, induces morphological changes and elicits apoptosis. hPAK65 is cleaved both in vitro and in vivo by caspases at a single site between the N-terminal regulatory p21-binding domain and the C-terminal kinase domain. The C-terminal cleavage prod- uct becomes activated, with a kinetic profile that parallels caspase activation during apoptosis. This C-terminal hPAK65 fragment also activates the c-Jun N-terminal kinase pathway in vivo.
机译:凋亡是细胞死亡的高度调控形式,其特征在于细胞收缩和核浓缩等独特特征。我们在这里证明了hPAK65,p21激活的激酶的蛋白水解激活诱导形态学变化并引发细胞凋亡。 hPAK65在体外和体内都被胱天蛋白酶在N端调节性p21结合结构域和C端激酶结构域之间的单个位点切割。 C末端裂解产物被激活,其动力学特征与凋亡期间胱天蛋白酶的激活平行。该C末端hPAK65片段还在体内激活c-Jun N末端激酶途径。

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