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题目:: DHHC protein-dependent palmitoylation protects regulator of G-protein signaling 4 from proteasome degradation.
作者:: Wang(Jincheng),Xie(Yan),Wolff(Dennis W),Abel(Peter W),Tu(Yaping)
状态:: 发布时间2010-11-15 , 更新时间 2016-11-22
期刊:: FEBS Lett
摘要:: Regulator of G-protein signaling 4 (RGS4), an intracellular modulator of G-protein coupled receptor (GPCR)-mediated signaling, is regulated by multiple processes including palmitoylation and proteasome degradation. We found that co-expression of DHHC acyltransferases (DHHC3 or DHHC7), but not their acyltransferase-inactive mutants, increased expression levels of RGS4 but not its Cys2 to Ser mutant (RGS4C2S). DHHC3 interacts with and palmitoylates RGS4 but not RGS4C2S in vivo. Palmitoylation prolongs the half-life of RGS4 by over 8-fold and palmitoylated RGS4 blocked α(1A)-adrenergic receptor-stimulated intracellular Ca(2+) mobilization. Together, our findings revealed that DHHC proteins could regulate GPCR-mediated signaling by increasing RGS4 stability.
语言:: eng
DOI:

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