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• W2079106772 abstract "Heterotrimeric G proteins in physiological and pathological processes have been extensively studied so far. However, little is known about mechanisms regulating the cellular content and compartmentalization of G proteins. Here, we show that the association of nucleoside diphosphate kinase B (NDPK B) with the G protein βγ dimer (Gβγ) is required for G protein function in vivo. In zebrafish embryos, morpholino-mediated knockdown of zebrafish NDPK B, but not NDPK A, results in a severe decrease in cardiac contractility. The depletion of NDPK B is associated with a drastic reduction in Gβ 1 γ 2 dimer expression. Moreover, the protein levels of the adenylyl cyclase (AC)-regulating Gα s and Gα i subunits as well as the caveolae scaffold proteins caveolin-1 and -3 are strongly reduced. In addition, the knockdown of the zebrafish Gβ 1 orthologs, Gβ 1 and Gβ 1like , causes a cardiac phenotype very similar to that of NDPK B morphants. The loss of Gβ 1 /Gβ 1like is associated with a down-regulation in caveolins, AC-regulating Gα-subunits, and most important, NDPK B. A comparison of embryonic fibroblasts from wild-type and NDPK A/B knockout mice demonstrate a similar reduction of G protein, caveolin-1 and basal cAMP content in mammalian cells that can be rescued by re-expression of human NDPK B. Thus, our results suggest a role for the interaction of NDPK B with Gβγ dimers and caveolins in regulating membranous G protein content and maintaining normal G protein function in vivo." @default.
• W2079106772 created "2016-06-24" @default.
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• W2079106772 date "2009-09-22" @default.
• W2079106772 modified "2023-10-14" @default.
• W2079106772 title "The interaction of nucleoside diphosphate kinase B with Gβγ dimers controls heterotrimeric G protein function" @default.
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• W2079106772 doi "https://doi.org/10.1073/pnas.0901679106" @default.
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