Serum-activated assembly and membrane translocation of an endogenous Rac1:effector complex
Serum-activated assembly and membrane translocation of an endogenous Rac1:effector complex
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DOI：
10.1016/s0960-9822(01)00091-4
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发表时间：
2001-03-06
期刊：
影响因子：
9.2
通讯作者：
Nelson, WJ
中科院分区：
文献类型：
--
作者：
Hansen, MDH;Nelson, WJ
Rho家族gtpase （Cdc42， Rac1和RhoA）在气体[1]下游发挥作用，并在各种细胞过程[2]中发挥作用，研究这些功能并没有直接将内源性蛋白质相互作用与Rho gtpase的特定体内功能联系起来。在这里，我们发现内源性Rad和两个已知的结合伙伴，Rho GDP解离抑制剂（RhoGDI）和p21活化激酶（PAK），作为不同的细胞质复合物分离。当细胞被血清激活时，Rac1:PAK复合物从细胞质转移到褶膜。过表达显性阴性（T17N） Rad并不影响该Rac1:PAK复合物的组装或分布。这是第一个直接证据，表明Rac1的特定功能是如何通过一个独特的Rac1效应复合体的组装和膜易位来选择的。2001爱思唯尔科学有限公司版权所有。
Rho family GTPases (Cdc42, Rac1, and RhoA) function downstream of gas [1], and in a variety of cellular processes [2], Studies to examine these functions have not directly linked endogenous protein interactions with specific in vivo functions of Rho GTPases, Here, we show that endogenous Rad and two known binding partners, Rho GDP dissociation inhibitor (RhoGDI) and p21-activated kinase (PAK), fractionate as distinct cytosolic complexes. A Rac1:PAK complex is translocated from the cytosol to ruffling membranes upon cell activation by serum. Overexpression of dominant-negative (T17N) Rad does not affect the assembly or distribution of this Rac1:PAK complex. This is the first direct evidence of how a specific function of Rac1 is selected by the assembly and membrane translocation of a distinct Rac1:effector complex. (C) 2001 Elsevier Science Ltd. All rights reserved.