Activation of RAC-protein kinase by heat shock and hyperosmolarity stress through a pathway independent of phosphatidylinositol 3-kinase

被引:188
作者
Konishi, H [1 ]
Matsuzaki, H [1 ]
Tanaka, M [1 ]
Ono, Y [1 ]
Tokunaga, C [1 ]
Kuroda, S [1 ]
Kikkawa, U [1 ]
机构
[1] KOBE UNIV,FAC SCI,DEPT BIOL,KOBE 657,JAPAN
关键词
pleckstrin homology domain; protein kinase C;
D O I
10.1073/pnas.93.15.7639
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
RAC protein kinase (RAC-PK), a serine/threonine protein kinase containing a pleckstrin homology (PH) domain, was activated by cellular stress such as heat shock and hyperosmolarity. Wortmannin, which is known as a potent inhibitor of phosphatidylinositol 3-kinase and normally inhibits growth factor-induced activation of RAC-PK, did not suppress heat-shock induced activation of RAC-PK, indicating that this stress-induced activation of the kinase is not mediated by phosphatidylinositol 3-kinase. The PH domain was indispensable for stress-induced activation of RAC-PK, In heat-treated cells, PKC delta, a member of the protein kinase C family, was found to associate with the PH domain of RAC-PK. This PKC subspecies was phosphorylated in vitro by RAC-PK. The results suggest that RAC-PK may play a role in the cellular response to stress through its PH domain.
引用
收藏
页码:7639 / 7643
页数:5
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