A BRAIN SERINE THREONINE PROTEIN-KINASE ACTIVATED BY CDC42 AND RAC1
A BRAIN SERINE THREONINE PROTEIN-KINASE ACTIVATED BY CDC42 AND RAC1
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DOI：
10.1038/367040a0
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发表时间：
1994-01-06
期刊：
影响因子：
64.8
通讯作者：
LIM, L
中科院分区：
文献类型：
--
作者：
MANSER, E;LEUNG, T;LIM, L
一种新的脑丝氨酸/苏氨酸蛋白激酶可能是p21 ras相关蛋白Cdc 42和Rac 1的靶点。激酶序列与酵母蛋白STE 20的序列相关，涉及信息素反应途径。该激酶与活化的（GTP结合的）p21特异性复合，抑制p21 GTP酶活性并导致激酶自磷酸化和活化。自磷酸化激酶对Cdc 42/Rac的亲和力降低，释放p21以进行进一步的刺激活性或被GTP酶激活蛋白下调。这种双分子相互作用为研究p21对哺乳动物磷酸化信号通路的调节提供了模型。
A new brain serine/threonine protein kinase may be a target for the p21ras-related proteins Cdc42 and Rac1. The kinase sequence is related to that of the yeast protein STE20, implicated in pheromone-response pathways. The kinase complexes specifically with activated (GTP-bound) p21, inhibiting p21 GTPase activity and leading to kinase autophosphorylation and activation. Autophosphorylated kinase has a decreased affinity for Cdc42/Rac, freeing the p21 for further stimulatory activities or downregulation by GTPase-activating proteins. This bimolecular interaction provides a model for studying p21 regulation of mammalian phosphorylation signalling pathways.