Abstract
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 summary: MINT- 8049215: Rgs4 (uniprotkb: P49799) physically interacts (MI: 0915) with DHHC3 (uniprotkb: Q8R173) by anti-tag coimmunoprecipitation (MI: 0007).
| Original language | English |
|---|---|
| Pages (from-to) | 4570-4574 |
| Number of pages | 5 |
| Journal | FEBS Letters |
| Volume | 584 |
| Issue number | 22 |
| DOIs | |
| State | Published - Nov 19 2010 |
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All Science Journal Classification (ASJC) codes
- Biochemistry
- Biophysics
- Cell Biology
- Genetics
- Molecular Biology
- Structural Biology
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DHHC protein-dependent palmitoylation protects regulator of G-protein signaling 4 from proteasome degradation. / Wang, Jincheng; Xie, Yan; Wolff, Dennis W.; Abel, Peter W.; Tu, Yaping.
In: FEBS Letters, Vol. 584, No. 22, 19.11.2010, p. 4570-4574.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - DHHC protein-dependent palmitoylation protects regulator of G-protein signaling 4 from proteasome degradation
AU - Wang, Jincheng
AU - Xie, Yan
AU - Wolff, Dennis W.
AU - Abel, Peter W.
AU - Tu, Yaping
PY - 2010/11/19
Y1 - 2010/11/19
N2 - 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 summary: MINT- 8049215: Rgs4 (uniprotkb: P49799) physically interacts (MI: 0915) with DHHC3 (uniprotkb: Q8R173) by anti-tag coimmunoprecipitation (MI: 0007).
AB - 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 summary: MINT- 8049215: Rgs4 (uniprotkb: P49799) physically interacts (MI: 0915) with DHHC3 (uniprotkb: Q8R173) by anti-tag coimmunoprecipitation (MI: 0007).
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UR - http://www.scopus.com/inward/citedby.url?scp=78249258095&partnerID=8YFLogxK
U2 - 10.1016/j.febslet.2010.10.052
DO - 10.1016/j.febslet.2010.10.052
M3 - Article
VL - 584
SP - 4570
EP - 4574
JO - FEBS Letters
JF - FEBS Letters
SN - 0014-5793
IS - 22
ER -