RGS11与其他RGS蛋白之间共享的一个G蛋白γ亚基样结构域决定了与Gβ5亚基的结合。
A G protein gamma subunit-like domain shared between RGS11 and other RGS proteins specifies binding to Gbeta5 subunits.
作者信息
Snow B E, Krumins A M, Brothers G M, Lee S F, Wall M A, Chung S, Mangion J, Arya S, Gilman A G, Siderovski D P
机构信息
Quantitative Biology Laboratory, Amgen Institute, Toronto, ON, Canada M5G 2C1.
出版信息
Proc Natl Acad Sci U S A. 1998 Oct 27;95(22):13307-12. doi: 10.1073/pnas.95.22.13307.
Abstract
Regulators of G protein signaling (RGS) proteins act as GTPase-activating proteins (GAPs) toward the alpha subunits of heterotrimeric, signal-transducing G proteins. RGS11 contains a G protein gamma subunit-like (GGL) domain between its Dishevelled/Egl-10/Pleckstrin and RGS domains. GGL domains are also found in RGS6, RGS7, RGS9, and the Caenorhabditis elegans protein EGL-10. Coexpression of RGS11 with different Gbeta subunits reveals specific interaction between RGS11 and Gbeta5. The expression of mRNA for RGS11 and Gbeta5 in human tissues overlaps. The Gbeta5/RGS11 heterodimer acts as a GAP on Galphao, apparently selectively. RGS proteins that contain GGL domains appear to act as GAPs for Galpha proteins and form complexes with specific Gbeta subunits, adding to the combinatorial complexity of G protein-mediated signaling pathways.
摘要
G蛋白信号调节（RGS）蛋白作为异源三聚体信号转导G蛋白α亚基的GTP酶激活蛋白（GAP）发挥作用。RGS11在其散乱蛋白/ Egl-10 /普列克底物蛋白结构域和RGS结构域之间含有一个G蛋白γ亚基样（GGL）结构域。在RGS6、RGS7、RGS9和秀丽隐杆线虫蛋白EGL-10中也发现了GGL结构域。RGS11与不同的Gβ亚基共表达揭示了RGS11与Gβ5之间的特异性相互作用。RGS11和Gβ5的mRNA在人体组织中的表达重叠。Gβ5 / RGS11异二聚体显然选择性地作为Gαo上的GAP发挥作用。含有GGL结构域的RGS蛋白似乎作为Gα蛋白的GAP发挥作用，并与特定的Gβ亚基形成复合物，增加了G蛋白介导的信号通路的组合复杂性。
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