In:
Science, American Association for the Advancement of Science (AAAS), Vol. 278, No. 5340 ( 1997-11-07), p. 1132-1135
Abstract:
Palmitoylation of the α subunit of the guanine nucleotide-binding protein G z inhibited by more than 90 percent its response to the guanosine triphosphatase (GTPase)–accelerating activity of G z GAP, a G z -selective member of the regulators of G-protein signaling (RGS) protein family of GTPase-activating proteins (GAPs). Palmitoylation both decreased the affinity of G z GAP for the GTP-bound form of Gα z by 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 Gα z also inhibited its response to the GAP activity of Gα-interacting protein (GAIP), another RGS protein, and palmitoylation of Gα i1 inhibited its response to RGS4. The extent of inhibition of G z GAP, 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 G z deactivation after its stimulation by receptors, and may be a general mechanism for prolonging or potentiating G-protein signaling.
Type of Medium:
Online Resource
ISSN:
0036-8075
,
1095-9203
DOI:
10.1126/science.278.5340.1132
Language:
English
Publisher:
American Association for the Advancement of Science (AAAS)
Publication Date:
1997
detail.hit.zdb_id:
128410-1
detail.hit.zdb_id:
2066996-3
detail.hit.zdb_id:
2060783-0
SSG:
11
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