Ignet

Gene Information

Gene symbol: RGS4

Gene name: regulator of G-protein signaling 4

HGNC ID: 10000

Related Genes

#	Gene Symbol	Number of hits
1	AGT	1 hits
2	BCL6	1 hits
3	INS	1 hits
4	PITX2	1 hits
5	PPARA	1 hits
6	RACGAP1	1 hits
7	RGS16	1 hits
8	RGS5	1 hits
9	RGS6	1 hits

Related Sentences

#	PMID	Sentence
1	12642593	Regulators of G-protein signaling (RGS) proteins down-regulate signaling by heterotrimeric G-proteins by accelerating GTP hydrolysis on the G alpha subunits.
2	12642593	For RGS16, mutation of Cys-2 and Cys-12 blocks its incorporation of [3H]palmitate and ability to turn-off Gi and Gq signaling and significantly inhibited its GTPase activating protein activity toward aG alpha subunit fused to the 5-hydroxytryptamine receptor 1A, but did not reduce its plasma membrane localization based on cell fractionation studies and immunoelectron microscopy.
3	12642593	However, disruption of lipid rafts by treatment with methyl-beta-cyclodextrin did not decrease the GTPase activating protein activity of RGS16.
4	12642593	The lipid raft fractions were enriched in protein acyltransferase activity, and RGS16 incorporated [3H]palmitate into a peptide fragment containing Cys-98, a highly conserved cysteine within the RGS box.
5	12642593	Chem. 278, 19309-19316) was critical for RGS16 and RGS4 GAP activity.
6	15313558	Palmitoylation can occur near the amino terminus, as for RGS4 and RGS16, but can also occur on a cysteine residue in the alpha4 helix of the RGS box, which is conserved in most RGS proteins.
7	15561937	We examined the role of abnormal G-protein activation in the pathogenesis of cardiac dysfunction by crossing PPAR-alpha mice with transgenic mice with cardiac-specific overexpression of regulator of G-protein signaling subtype 4 (RGS4), a GTPase activating protein for Gq and Gi.
8	15561937	Generation of compound transgenic mice demonstrated that cardiac RGS4 overexpression ameliorated the cardiomyopathic phenotype that occurred as a result of PPAR-alpha overexpression without affecting the metabolic abnormalities seen in these hearts.
9	15561937	We examined the role of abnormal G-protein activation in the pathogenesis of cardiac dysfunction by crossing PPAR-alpha mice with transgenic mice with cardiac-specific overexpression of regulator of G-protein signaling subtype 4 (RGS4), a GTPase activating protein for Gq and Gi.
10	15561937	Generation of compound transgenic mice demonstrated that cardiac RGS4 overexpression ameliorated the cardiomyopathic phenotype that occurred as a result of PPAR-alpha overexpression without affecting the metabolic abnormalities seen in these hearts.
11	18337495	Activation of the nuclear hormone receptor peroxisome proliferator-activated receptor delta (PPARdelta) has been shown to improve insulin resistance, adiposity, and plasma HDL levels.
12	18337495	Here we report atheroprotective effects of PPARdelta activation in a model of angiotensin II (AngII)-accelerated atherosclerosis, characterized by increased vascular inflammation related to repression of an antiinflammatory corepressor, B cell lymphoma-6 (Bcl-6), and the regulators of G protein-coupled signaling (RGS) proteins RGS4 and RGS5.
13	18337495	In this model, administration of the PPARdelta agonist GW0742 (1 or 10 mg/kg) substantially attenuated AngII-accelerated atherosclerosis without altering blood pressure and increased vascular expression of Bcl-6, RGS4, and RGS5, which was associated with suppression of inflammatory and atherogenic gene expression in the artery.
14	18337495	In vitro studies demonstrated similar changes in AngII-treated macrophages: PPARdelta activation increased both total and free Bcl-6 levels and inhibited AngII activation of MAP kinases, p38, and ERK1/2.
15	18337495	Activation of the nuclear hormone receptor peroxisome proliferator-activated receptor delta (PPARdelta) has been shown to improve insulin resistance, adiposity, and plasma HDL levels.
16	18337495	Here we report atheroprotective effects of PPARdelta activation in a model of angiotensin II (AngII)-accelerated atherosclerosis, characterized by increased vascular inflammation related to repression of an antiinflammatory corepressor, B cell lymphoma-6 (Bcl-6), and the regulators of G protein-coupled signaling (RGS) proteins RGS4 and RGS5.
17	18337495	In this model, administration of the PPARdelta agonist GW0742 (1 or 10 mg/kg) substantially attenuated AngII-accelerated atherosclerosis without altering blood pressure and increased vascular expression of Bcl-6, RGS4, and RGS5, which was associated with suppression of inflammatory and atherogenic gene expression in the artery.
18	18337495	In vitro studies demonstrated similar changes in AngII-treated macrophages: PPARdelta activation increased both total and free Bcl-6 levels and inhibited AngII activation of MAP kinases, p38, and ERK1/2.
19	20385802	RGS4 is a negative regulator of insulin release from pancreatic beta-cells in vitro and in vivo.
20	20385802	At present, it remains unknown whether RGS proteins play a role in regulating insulin release.
21	20385802	To address this issue, we initially demonstrated that MIN6 insulinoma cells express functional M3Rs and that RGS4 was by far the most abundant RGS protein expressed by these cells.
22	20385802	Interestingly, RGS4 deficiency had little effect on insulin release caused by activation of other beta-cell GPCRs.
23	20385802	Finally, treatment of mutant mice selectively lacking RGS4 in pancreatic beta-cells with a muscarinic agonist (bethanechol) led to significantly increased plasma insulin and reduced blood glucose levels, as compared to control littermates.
24	20385802	These findings indicate that RGS4 is a potent negative regulator of M3R function in pancreatic beta-cells, suggesting that RGS4 may represent a potential target to promote insulin release for therapeutic purposes.
25	20385802	RGS4 is a negative regulator of insulin release from pancreatic beta-cells in vitro and in vivo.
26	20385802	At present, it remains unknown whether RGS proteins play a role in regulating insulin release.
27	20385802	To address this issue, we initially demonstrated that MIN6 insulinoma cells express functional M3Rs and that RGS4 was by far the most abundant RGS protein expressed by these cells.
28	20385802	Interestingly, RGS4 deficiency had little effect on insulin release caused by activation of other beta-cell GPCRs.
29	20385802	Finally, treatment of mutant mice selectively lacking RGS4 in pancreatic beta-cells with a muscarinic agonist (bethanechol) led to significantly increased plasma insulin and reduced blood glucose levels, as compared to control littermates.
30	20385802	These findings indicate that RGS4 is a potent negative regulator of M3R function in pancreatic beta-cells, suggesting that RGS4 may represent a potential target to promote insulin release for therapeutic purposes.
31	20385802	RGS4 is a negative regulator of insulin release from pancreatic beta-cells in vitro and in vivo.
32	20385802	At present, it remains unknown whether RGS proteins play a role in regulating insulin release.
33	20385802	To address this issue, we initially demonstrated that MIN6 insulinoma cells express functional M3Rs and that RGS4 was by far the most abundant RGS protein expressed by these cells.
34	20385802	Interestingly, RGS4 deficiency had little effect on insulin release caused by activation of other beta-cell GPCRs.
35	20385802	Finally, treatment of mutant mice selectively lacking RGS4 in pancreatic beta-cells with a muscarinic agonist (bethanechol) led to significantly increased plasma insulin and reduced blood glucose levels, as compared to control littermates.
36	20385802	These findings indicate that RGS4 is a potent negative regulator of M3R function in pancreatic beta-cells, suggesting that RGS4 may represent a potential target to promote insulin release for therapeutic purposes.
37	20385802	RGS4 is a negative regulator of insulin release from pancreatic beta-cells in vitro and in vivo.
38	20385802	At present, it remains unknown whether RGS proteins play a role in regulating insulin release.
39	20385802	To address this issue, we initially demonstrated that MIN6 insulinoma cells express functional M3Rs and that RGS4 was by far the most abundant RGS protein expressed by these cells.
40	20385802	Interestingly, RGS4 deficiency had little effect on insulin release caused by activation of other beta-cell GPCRs.
41	20385802	Finally, treatment of mutant mice selectively lacking RGS4 in pancreatic beta-cells with a muscarinic agonist (bethanechol) led to significantly increased plasma insulin and reduced blood glucose levels, as compared to control littermates.
42	20385802	These findings indicate that RGS4 is a potent negative regulator of M3R function in pancreatic beta-cells, suggesting that RGS4 may represent a potential target to promote insulin release for therapeutic purposes.
43	20385802	RGS4 is a negative regulator of insulin release from pancreatic beta-cells in vitro and in vivo.
44	20385802	At present, it remains unknown whether RGS proteins play a role in regulating insulin release.
45	20385802	To address this issue, we initially demonstrated that MIN6 insulinoma cells express functional M3Rs and that RGS4 was by far the most abundant RGS protein expressed by these cells.
46	20385802	Interestingly, RGS4 deficiency had little effect on insulin release caused by activation of other beta-cell GPCRs.
47	20385802	Finally, treatment of mutant mice selectively lacking RGS4 in pancreatic beta-cells with a muscarinic agonist (bethanechol) led to significantly increased plasma insulin and reduced blood glucose levels, as compared to control littermates.
48	20385802	These findings indicate that RGS4 is a potent negative regulator of M3R function in pancreatic beta-cells, suggesting that RGS4 may represent a potential target to promote insulin release for therapeutic purposes.