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一种由Cdc42和Rac1激活的脑丝氨酸/苏氨酸蛋白激酶。

A brain serine/threonine protein kinase activated by Cdc42 and Rac1.

作者信息

Manser E, Leung T, Salihuddin H, Zhao Z S, Lim L

机构信息

Institute of Molecular & Cell Biology, National University of Singapore, Kent Ridge.

出版信息

Nature. 1994 Jan 6;367(6458):40-6. doi: 10.1038/367040a0.

Abstract

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.

摘要

一种新的脑丝氨酸/苏氨酸蛋白激酶可能是与p21ras相关蛋白Cdc42和Rac1的作用靶点。该激酶序列与酵母蛋白STE20的序列相关,STE20参与信息素应答途径。该激酶与活化的(结合GTP的)p21特异性结合,抑制p21 GTP酶活性,并导致激酶自身磷酸化和激活。自身磷酸化的激酶对Cdc42/Rac的亲和力降低,使p21得以释放,用于进一步的刺激活动或被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一个模型。

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