Lipid modifications of G protein subunits.
1991; Elsevier BV; Volume: 266; Issue: 7 Linguagem: Inglês
10.1016/s0021-9258(20)64372-1
ISSN1083-351X
AutoresMaurine E. Linder, Iok-Hou Pang, Robert J. Duronio, Jeffrey I. Gordon, Paul C. Sternweis, Alfred G. Gilman,
Tópico(s)Metabolism and Genetic Disorders
ResumoExpression of the G protein subunit G, in this system results in the synthesis of two forms of the protein; these were separated on a column of heptylamine-Sepharose.Purification of the more abundant form of Go, yielded a product that has a blocked amino terminus.Chemical analysis of the fatty acids released by acid hydrolysis of the protein revealed myristic acid.The second form of the protein was not myristoylated.Myristoylated and nonmyristoylated recombinant Go, were compared with brain Go, (which is myristoylated) for their ability to interact with G protein By subunits.The nonmyristoylated recombinant protein clearly had a reduced affinity for By, while the myristoylated recombinant protein was indistinguishable from native G, in its subunit interactions.Thus, myristoylation increases the affinity of a subunits for By.We propose that the function of myristoylation of G protein a subunits is, at least in part, to facilitate formation of the heterotrimer and the localization of a to the plasma membrane.Members of a family of guanine nucleotide-binding regulatory proteins (G proteins)' serve as transducers in a variety
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