The core domain of RGS16 retains G-protein binding and GAP activity in vitro, but is not functional in vivo

被引：33

作者：

Chen, CH ^{[1
]}

Lin, SC ^{[1
]}

机构：

[1] Natl Univ Singapore, Inst Mol & Cell Biol, Regulatory Biol Lab, Singapore 117609, Singapore

来源：

FEBS LETTERS | 1998年 / 422卷 / 03期

关键词：

RGS protein; RGS16; GTP-binding protein; GTPase-activating protein;

D O I：

10.1016/S0014-5793(98)00042-8

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The regulators of G-protein signaling (RGS) family members contain a conserved region, the RGS domain, and are GTPase-activating proteins for many members of G-protein alpha-subunits, We report here that the core domain of RGS16 is sufficient for in vitro biochemical functions as assayed by its G-protein binding affinity and its ability to stimulate GTP hydrolysis by G alpha(o) protein, RGS16 also requires, in addition to the RGS domain, the divergent N-terminus for its biological function in the attenuation of pheromone signaling in yeast, whereas its C-terminus region is dispensable, Together with other evidence, these data support the notion that RGS proteins interact with other cellular factors and may serve to link specific G-proteins to different downstream effecters in G-protein-mediated signaling pathways. (C) 1998 Federation of European Biochemical Societies.

引用

页码：359 / 362

页数：4

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