کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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2049213 | 1074120 | 2010 | 5 صفحه PDF | دانلود رایگان |
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 α1A-adrenergic receptor-stimulated intracellular Ca2+ mobilization. Together, our findings revealed that DHHC proteins could regulate GPCR-mediated signaling by increasing RGS4 stability.Structured summaryMINT-8049215: Rgs4 (uniprotkb:P49799) physically interacts (MI:0915) with DHHC3 (uniprotkb:Q8R173) by anti-tag coimmunoprecipitation (MI:0007)
Journal: FEBS Letters - Volume 584, Issue 22, 19 November 2010, Pages 4570–4574