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Genetic and structural analysis of G protein α subunit regulatory domains

✍ Scribed by Gary L. Johnson; N. Dhanasekaran; Sunil K. Gupta; Joseph M. Lowndes; Richard R. Vaillancourt; Arnold E. Ruoho

Publisher
John Wiley and Sons
Year
1991
Tongue
English
Weight
994 KB
Volume
47
Category
Article
ISSN
0730-2312

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✦ Synopsis

Genetic and structural analysis of the a chain polypeptides of heterotrimeric G proteins defines functional domains for GTP/GDP binding, GTPase activity, effector activation, receptor contact and Pr subunit complex regulation. The conservation in sequence comprising the GDP/GTP binding and GTPase domains among G protein cx subunits readily allows common mutations to be made for the design of mutant polypeptides that function as constitutive active or dominant negative a chains when expressed in different cell types. Organization of the effector activation, receptor and Pr contact domains is similar in the primary sequence of the different (Y subunit polypeptides relative to the GTP/GDP binding domain sequences. Mutation within common motifs of the different G protein a chain polypeptides have similar functional consequences. Thus, what has been learned with the Gs and Gi proteins and the regulation of adenylyl cyclase can be directly applied to the analysis of newly identified G proteins and their coupling to receptors and regulation of putative effector enzymes.

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