期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1999
卷号：96
期号：11
页码：6489-6494
DOI：10.1073/pnas.96.11.6489
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：Several regulators of G protein signaling (RGS) proteins contain a G protein {gamma}-subunit-like (GGL) domain, which, as we have shown, binds to G{beta}5 subunits. Here, we extend our original findings by describing another GGL-domain-containing RGS, human RGS6. When RGS6 is coexpressed with different G{beta} subunits, only RGS6 and G{beta}5 interact. The expression of mRNA for RGS6 and G{beta}5 in human tissues overlaps. Predictions of -helical and coiled-coil character within GGL domains, coupled with measurements of G{beta} binding by GGL domain mutants, support the contention that G{gamma}-like regions within RGS proteins interact with G{beta}5 subunits in a fashion comparable to conventional G{beta}/G{gamma} pairings. Mutation of the highly conserved Phe-61 residue of G{gamma}2 to tryptophan, the residue present in all GGL domains, increases the stability of the G{beta}5/G{gamma}2 heterodimer, highlighting the importance of this residue to GGL/G{beta}5 association.
