Ignet

Gene Information

Gene symbol: RGS6

Gene name: regulator of G-protein signaling 6

HGNC ID: 10002

Related Genes

#	Gene Symbol	Number of hits
1	INS	1 hits
2	PITX2	1 hits
3	RAC1	1 hits
4	RACGAP1	1 hits
5	RGS16	1 hits
6	RGS4	1 hits
7	RGS7	1 hits
8	SUCLG2	1 hits

Related Sentences

#	PMID	Sentence
1	10648734	Copurification of brain G-protein beta5 with RGS6 and RGS7.
2	10648734	The copurifying 55 kDa band was identified as an approximately 1:1 mixture of RGS6 and RGS7 by matrix-assisted laser desorption ionization mass spectroscopic analysis of tryptic peptides.
3	10648734	These findings implicate RGS6 and RGS7 in the function of Gbeta5 in the brain and suggest that a large fraction of membrane-targeted Gbeta5 has no associated G subunit and therefore functions outside the canonical framework of G(beta)(gamma) interactions.
4	10648734	Copurification of brain G-protein beta5 with RGS6 and RGS7.
5	10648734	The copurifying 55 kDa band was identified as an approximately 1:1 mixture of RGS6 and RGS7 by matrix-assisted laser desorption ionization mass spectroscopic analysis of tryptic peptides.
6	10648734	These findings implicate RGS6 and RGS7 in the function of Gbeta5 in the brain and suggest that a large fraction of membrane-targeted Gbeta5 has no associated G subunit and therefore functions outside the canonical framework of G(beta)(gamma) interactions.
7	10648734	Copurification of brain G-protein beta5 with RGS6 and RGS7.
8	10648734	The copurifying 55 kDa band was identified as an approximately 1:1 mixture of RGS6 and RGS7 by matrix-assisted laser desorption ionization mass spectroscopic analysis of tryptic peptides.
9	10648734	These findings implicate RGS6 and RGS7 in the function of Gbeta5 in the brain and suggest that a large fraction of membrane-targeted Gbeta5 has no associated G subunit and therefore functions outside the canonical framework of G(beta)(gamma) interactions.
10	12642593	Regulators of G-protein signaling (RGS) proteins down-regulate signaling by heterotrimeric G-proteins by accelerating GTP hydrolysis on the G alpha subunits.
11	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.
12	12642593	However, disruption of lipid rafts by treatment with methyl-beta-cyclodextrin did not decrease the GTPase activating protein activity of RGS16.
13	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.
14	12642593	Chem. 278, 19309-19316) was critical for RGS16 and RGS4 GAP activity.
15	21907914	Apart from their classical mechanism of action as GTPase-activating proteins (GAPs), RGS proteins can also serve other noncanonical functions.
16	21907914	As more reports are being published on this group of proteins, it is becoming clear that modulation of GAP activity might not be the only way to therapeutically target RGS proteins.
17	21907914	Apart from their classical mechanism of action as GTPase-activating proteins (GAPs), RGS proteins can also serve other noncanonical functions.
18	21907914	As more reports are being published on this group of proteins, it is becoming clear that modulation of GAP activity might not be the only way to therapeutically target RGS proteins.
19	21969604	Insulin exerts many of its metabolic actions via the canonical phosphatidylinositide 3 kinase (PI3K)/Akt pathway, leading to phosphorylation and 14-3-3 binding of key metabolic targets.
20	21969604	We previously identified a GTPase-activating protein (GAP) for Rac1 called RhoGAP22 as an insulin-responsive 14-3-3 binding protein.
21	21969604	Insulin increased 14-3-3 binding to RhoGAP22 fourfold, and this effect was PI3K dependent.
22	21969604	Mutation of the catalytic arginine of the GAP domain of RhoGAP22 potentiated growth factor-stimulated Rac1 GTP loading.
23	21969604	We propose that insulin and possibly growth factors such as platelet-derived growth factor may play a novel role in regulating cell migration and motility via the Akt-dependent phosphorylation of RhoGAP22, leading to modulation of Rac1 activity.
24	21969604	Insulin exerts many of its metabolic actions via the canonical phosphatidylinositide 3 kinase (PI3K)/Akt pathway, leading to phosphorylation and 14-3-3 binding of key metabolic targets.
25	21969604	We previously identified a GTPase-activating protein (GAP) for Rac1 called RhoGAP22 as an insulin-responsive 14-3-3 binding protein.
26	21969604	Insulin increased 14-3-3 binding to RhoGAP22 fourfold, and this effect was PI3K dependent.
27	21969604	Mutation of the catalytic arginine of the GAP domain of RhoGAP22 potentiated growth factor-stimulated Rac1 GTP loading.
28	21969604	We propose that insulin and possibly growth factors such as platelet-derived growth factor may play a novel role in regulating cell migration and motility via the Akt-dependent phosphorylation of RhoGAP22, leading to modulation of Rac1 activity.