Inhibition of brain Gz GAP and other RGS proteins by palmitoylation of G protein alpha subunits.

Inhibition of brain Gz GAP and other RGS proteins by palmitoylation of G protein alpha subunits.
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通过 G 蛋白 α 亚基的棕榈酰化来抑制大脑 Gz GAP 和其他 RGS 蛋白。

DOI:
10.1126/science.278.5340.1132
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发表时间:
1997
期刊:
Science (New York, N.Y.)
影响因子:
--
通讯作者:
Ross,EM
Ross,EM
中科院分区:
--
文献类型:
--
作者:
Tu,Y;Wang,J;Ross,EM

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Palmitoylation of the α subunit of the guanine nucleotide-binding protein Gzinhibited by more than 90 percent its response to the guanosine triphosphatase (GTPase)–accelerating activity of GzGAP, a Gz-selective member of the regulators of G-protein signaling (RGS) protein family of GTPase-activating proteins (GAPs). Palmitoylation both decreased the affinity of GzGAP for the GTP-bound form of Gαzby at least 90 percent and decreased the maximum rate of GTP hydrolysis. Inhibition was reversed by removal of the palmitoyl group by dithiothreitol. Palmitoylation of Gαzalso inhibited its response to the GAP activity of Gα-interacting protein (GAIP), another RGS protein, and palmitoylation of Gαi1inhibited its response to RGS4. The extent of inhibition of GzGAP, GAIP, RGS4, and RGS10 correlated roughly with their intrinsic GAP activities for the Gα target used in the assay. Reversible palmitoylation is thus a major determinant of Gzdeactivation after its stimulation by receptors, and may be a general mechanism for prolonging or potentiating G-protein signaling.
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