| First Author | Wang J | Year | 2010 |
| Journal | FEBS Lett | Volume | 584 |
| Issue | 22 | Pages | 4570-4 |
| PubMed ID | 21035448 | Mgi Jnum | J:166146 |
| Mgi Id | MGI:4839836 | Doi | 10.1016/j.febslet.2010.10.052 |
| Citation | Wang J, et al. (2010) DHHC protein-dependent palmitoylation protects regulator of G-protein signaling 4 from proteasome degradation. FEBS Lett 584(22):4570-4 |
| abstractText | 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 alpha(1A)-adrenergic receptor-stimulated intracellular Ca(2+) mobilization. Together, our findings revealed that DHHC proteins could regulate GPCR-mediated signaling by increasing RGS4 stability. |
