The regulators of G protein signaling (RGS) domains of RGS4, RGS10, and GAIP retain GTPase activating protein activity in vitro.
The regulators of G protein signaling (RGS) domains of RGS4, RGS10, and GAIP retain GTPase activating protein activity in vitro.
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DOI：
10.1073/pnas.94.14.7216
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发表时间：
1997-07
影响因子：
11.1
通讯作者：
S. Popov;Kan Yu;T. Kozasa;T. Wilkie
中科院分区：
文献类型：
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作者：
S. Popov;Kan Yu;T. Kozasa;T. Wilkie
G蛋白信号调节蛋白（RGS）可加速Gi（抑制型G蛋白）的GTP水解，但不加速Gs（激活型G蛋白）类α亚基的GTP水解。所有的RGS蛋白都有一个由120个氨基酸组成的保守序列，被称为RGS结构域。我们已经证明，RGS4、RGS10和GAIP的RGS结构域在体外对Gi类底物Gialpha1、Goalpha和Gzalpha保留有GTP酶加速活性。未检测到RGS结构域对Gsalpha有调节活性。RGS4的RGS结构域内的短缺失破坏了GTP酶激活蛋白活性以及与Gialpha1底物的结合。利用表面等离子体共振技术检测到了Gialpha1 - GDP - AlF4 - 与RGS结构域或全长RGS4之间类似的蛋白质 - 蛋白质相互作用。
Regulators of G protein signaling (RGS) proteins accelerate GTP hydrolysis by Gi but not by Gs class alpha-subunits. All RGS proteins share a conserved 120-amino acid sequence termed the RGS domain. We have demonstrated that the RGS domains of RGS4, RGS10, and GAIP retain GTPase accelerating activity with the Gi class substrates Gialpha1, Goalpha, and Gzalpha in vitro. No regulatory activity of the RGS domains was detected for Gsalpha. Short deletions within the RGS domain of RGS4 destroyed GTPase activating protein activity and Gialpha1 substrate binding. Comparable protein-protein interactions between Gialpha1-GDP-AlF4- and the RGS domain or full-length RGS4 were detected using surface plasmon resonance.