ライフサイエンスコーパス: RGS

1 RGS (regulator of G protein signaling) proteins are nega

2 RGS (regulator of G protein signaling) proteins of the R

3 RGS proteins are best understood as negative regulators

4 RGS proteins are subject to posttranslational modificati

5 RGS proteins exert their effect by directly binding to t

6 RGS proteins interact with, and affect the activity of,

7 RGS proteins limit the duration that Galphai subunits re

8 RGS proteins stimulate the deactivation of heterotrimeri

9 RGS-containing RhoGEFs (RGS-RhoGEFs) represent a direct

10 RGS-insensitive mice were also 5-10 times more responsiv

11 f these small-molecule inhibitors against 12 RGS proteins, as well as against the cysteine-null mutan

12 s and that RGS4 was by far the most abundant RGS protein expressed by these cells.

13 ve NFR1 receptors phosphorylate and activate RGS proteins, which help maintain the Galpha proteins in

14 All RGS proteins share a common RGS domain that interacts wi

15 ai2 (G184S/G184S) mutation that disables all RGS protein/Galphai2 interactions exhibit an unexpectedl

16 Alternatively, RGS proteins might also have a direct role in regulating

17 Although RGS proteins canonically function as G-protein regulator

18 They show selectivity among RGS proteins with a potency order of RGS 4 > 19 = 16 > 8

19 do this, a knock-in mouse that expresses an RGS-insensitive (RGSi) mutant Galphao protein, Galphao(G

20 ng) protein AtRGS1, which is comprised of an RGS domain fused to a receptor-like domain.

21 Pases in the intracellular trafficking of an RGS protein.

22 h the GEF activity of p115-RhoGEF (p115), an RGS-RhoGEF, can be stimulated by Galpha(13), the exact m

23 RGS14 possesses an RGS domain that binds active Galpha(i/o)-GTP subunits to

24 Experiments with pertussis toxin, an RGS domain-deficient mutant of RGS7, and UBO-QIC {L-thre

25 ich has the largest complement of Galpha and RGS proteins for any eukaryote, provides new insights in

26 yses and homology modeling of the Galpha and RGS proteins to address their expansion and its potentia

27 eraction between the cognate GPCR (Mam2) and RGS (Rgs1), mapping the interaction domains.

28 At neuronal synapses, GPCRs, G proteins, and RGS proteins work in coordination to regulate key aspect

29 ctions between activated Galpha subunits and RGS proteins have yielded a substantial number of inhibi

30 he development of the kidney vasculature and RGS (regulator of G-protein signaling) genes, suggesting

31 signaling enhances the expression of another RGS domain-containing protein, PDZ-RGS3.

32 es the selectivity of commercially available RGS inhibitors and provides insight into the RGS family

33 onte Carlo simulation of the probe for beta- RGS, the activity that is to be administered for a succe

34 ins compatible with the application of beta- RGS.

35 The application of this beta- RGS to neuroendocrine tumors (NET) requires study of the

36 G184S substitution in G(i2alpha) that blocks RGS/G(i2) interactions to examine the consequences of li

37 on that Galpha(i) subunits remain GTP bound, RGS proteins modulate chemoattractant receptor signaling

38 the Galpha subunit, a reaction catalyzed by RGS proteins.

39 d blunting of sensitivity also engendered by RGS protein action in trans.

40 ity of the G-protein signaling regulation by RGS.Gbeta5 complexes achieved by differential recruitmen

41 ) is a member of a family of proteins called RGS proteins, which function as GTPase-activating protei

42 regulation, and functional role of canonical RGS proteins, with a special focus on the healthy heart

43 The soybean genome encodes two chimeric RGS proteins with an N-terminal seven transmembrane doma

44 rotein is readily inactivated by its cognate RGS protein and forms a stable, GDP-bound, heterotrimeri

45 All RGS proteins share a common RGS domain that interacts with G protein alpha subunits

46 subcellular localization to compartmentalize RGS activity within a cell, thus highlighting their impo

47 phobic motifs in RH outside of the consensus RGS box are critical for this process.

48 In a cellular context, RGS proteins have also been shown to speed up the onset

49 merization system that enabled us to control RGS localization independent from R7BP in living cells.

50 ne-driven ON-BCs are determined by different RGS concentrations.

51 cytes with a Galphai2 mutation that disables RGS protein binding accumulated in the perivascular chan

52 ed on the opposite face of RGS4, can disrupt RGS/Galpha interaction through an allosteric mechanism t

53 s to evaluate the contribution of endogenous RGS proteins to the antinociceptive effects of morphine

54 eins from species with or without endogenous RGS.

55 may prove to be an effective way to enhance RGS protein function.

56 in meningiomas but was still acceptable for RGS, particularly if further research and development ar

57 s that the tracer can still be effective for RGS.

58 Our results strongly support a role for RGS proteins as negative regulators of opioid supraspina

59 ese findings establish an essential role for RGS proteins in B cell chemoattractant signaling and for

60 ervations (1) demonstrate an active role for RGS proteins in regulating platelet responsiveness, (2)

61 ly been identified as an allosteric site for RGS regulation by acidic phospholipids.

62 ical and cell-based methods to assess Galpha-RGS complex formation and Galpha enzymatic activity, we

63 hereby responsible for selectivity in Galpha-RGS interactions.

64 m that almost completely inhibits the Galpha-RGS protein-protein interaction.

65 t for the adaptive coevolution of the Galpha:RGS protein pair based on single amino acid substitution

66 ion-based adaptive coevolution of the Galpha:RGS proteins was proposed to enable the loss of RGS in m

67 Both Gbetagamma and Gbeta5-RGS are obligate dimers that are thought to require the

68 extends previous attempts by including GPCR-RGS interactions.

69 In vivo and in silico data confirm that GPCR-RGS interactions can impose an additional layer of regul

70 a regulator of G protein signaling homology (RGS) domain.

71 This study reveals how RGS proteins modulate Galphai2 signaling to facilitate t

72 proteins, it is important to understand how RGS regulates selective GPCR-G protein signaling.

73 However, RGS proteins differ widely in size and the organization

74 etection and resection during first-in-human RGS.

75 We further show that changes in RGS concentration differentially impact visually guided-

76 is approach was used to correlate changes in RGS localization and activity in the presence or absence

77 se and heart rate regulation, and changes in RGS protein expression and/or function are believed to p

78 n to permit either increases or decreases in RGS function.

79 ise from the consensus GoLoco motif found in RGS proteins.

80 siological states, so strategies to increase RGS function would be useful.

81 ain GTP bound, and the loss of an individual RGS protein typically enhances chemokine receptor signal

82 leic acid downregulation of IKACh-inhibiting RGS proteins was present at 16 weeks.

83 or any eukaryote, provides new insights into RGS function and evolution.

84 endrites by varying the concentration of key RGS proteins and measuring the impact on transmission of

85 t is unclear which of the more than 20 known RGS proteins function to negatively regulate and thereby

86 terations in the PX domains of the mammalian RGS-PX proteins, SNX13, SNX14, SNX19, and SNX25, confer

87 Many RGS proteins also bind additional signaling partners tha

88 However, many RGS proteins contain additional domains that serve other

89 tional layer of regulation through mediating RGS subcellular localization to compartmentalize RGS act

90 brane anchoring subunit or further modulates RGS proteins to increase their GAP activity.

91 doate], a previously reported small-molecule RGS inhibitor.

92 Unlike previous small-molecule RGS inhibitors identified to date, these compounds retai

93 inhibitors display activity toward multiple RGS family members.

94 Neutrophil RGS proteins establish a threshold for Galpha(i) activat

95 of RGS9.Gbeta5 and enhancing the ability of RGS.Gbeta5 complexes to stimulate GTPase activity of G p

96 ors to pheromone signaling in the absence of RGS-mediated GAP activity.

97 an essential role for modulatory actions of RGS proteins in adult cerebellum.

98 rotein cycle is regulated by the activity of RGS proteins.

99 membrane interactions in spatial control of RGS-PX proteins in cell signaling and trafficking.

100 The diversity of RGS domains from Naegleria in particular, which has the

101 rmore, this newly characterized diversity of RGS domains helps in defining their ancestral conserved

102 understanding of the molecular diversity of RGS proteins that control MOR signaling, their circuit s

103 With hundreds of GPCRs and dozens of RGS proteins, compartmentalization plays a key role in e

104 These results reveal the existence of RGS protein homo-oligomers and show regulation of their

105 Lower or higher expression of RGS proteins results in fewer or more nodules, respectiv

106 nd also reveal a potential novel function of RGS proteins as positive regulators of opioid spinal ant

107 ctivity, to mimic in cis the GAP function of RGS proteins.

108 n this paper, we report that the R7 group of RGS regulators is controlled by interaction with two pre

109 neficial effects of serotonin, inhibition of RGS proteins represents a therapeutic approach for the t

110 We propose that the interaction of RGS proteins with orphan GPCRs promotes signaling select

111 s may exist which compensate for the loss of RGS in certain plant species.

112 proteins was proposed to enable the loss of RGS in monocots.

113 s there are concomitant, independent LSEs of RGS proteins along with an extraordinary diversification

114 Most studies searching for modulators of RGS protein function have been focused on inhibiting the

115 al mushrooms show LSEs of Galphas but not of RGS proteins pointing to the probable differentiation of

116 y among RGS proteins with a potency order of RGS 4 > 19 = 16 > 8 >> 7.

117 urface expression and through recruitment of RGS proteins.

118 indings reveal a hitherto overlooked role of RGS proteins as noise suppressors and demonstrate an abi

119 velopment of chemical tools for the study of RGS physiology.

120 Although the R4 subfamily of RGS proteins generally accepts both Galphai/o and Galpha

121 GS7 and RGS9-2 belong to the R7 subfamily of RGS proteins that form macromolecular complexes with R7-

122 entify RGS6, a member of the R7 subfamily of RGS proteins, as a key regulator of GABA(B)R signaling i

123 uss a rationale for therapeutic targeting of RGS proteins by regulation of expression or allosteric m

124 el of night blindness prevented targeting of RGS to the postsynaptic compartment of bipolar neurons i

125 Septin organization is dependent on RGS protein activity.

126 one Galpha, one Gbeta, three Ggamma, and one RGS protein.

127 In contrast, only one RGS protein, RGS2, is known to be selective for Galphaq/

128 ed RGS4 inhibitors were active against other RGS members, such as RGS14, with comparable or greater p

129 Like other RGS (regulator of G protein signaling) proteins, RGS14 a

130 midbrain expression and trafficking of other RGS proteins such as RGS4 and RGS8.

131 However, unlike other RGS proteins, RGS14 also contains a G protein regulatory

132 Analysis of phosphorylated RGS protein identifies specific amino acids that, when p

133 , while G-proteins are widespread in plants, RGS proteins have been reported to be missing from the e

134 vity toward RhoA, these RhoGEFs also possess RGS homology (RH) domains that interact with activated a

135 s, RGS6-Gbeta5, but not RGS4, is the primary RGS modulator of parasympathetic HR regulation and SAN M

136 used with liver NET metastases, the proposed RGS technique is believed to be feasible by injecting an

137 R7 RGS proteins contain several distinct domains and form o

138 Rgs6(-/-) mice is attributable to another R7 RGS protein whose influence on M2R-IKACh signaling is ma

139 rane compartments, dissociated R7BP-bound R7 RGS complexes from Gi/o-gated G protein-regulated inward

140 ane and facilitating Gi/o deactivation by R7 RGS proteins on GIRK channels.

141 ervous system, is mediated exclusively by R7 RGS proteins.

142 and show regulation of their assembly by R7 RGS-binding partners.

143 ain of R7 RGS proteins, and mutant Gbeta5-R7 RGS complexes initially formed in cells but were then ra

144 nctional importance, the mechanism of how R7 RGS forms complexes with Gbeta5 and membrane anchors rem

145 e are key to controlling the stability of R7 RGS protein complexes.

146 , a palmitoylated allosteric modulator of R7 RGS proteins that accelerate deactivation of Gi/o class

147 se findings argue that the association of R7 RGS proteins with the membrane environment provides a ma

148 o still bind the N-terminal DEP domain of R7 RGS proteins, and mutant Gbeta5-R7 RGS complexes initial

149 Rs (MOR and D2R) on the G protein bias of R7 RGS proteins.

150 ta5 complexes under allosteric control of R7 RGS-binding protein (R7BP).

151 All members of the R7 RGS form trimeric complexes with the atypical G protein

152 5 that selectively destabilize one of the R7 RGS proteins in Caenorhabditis elegans.

153 maintaining proteolytic stability of the R7 RGS proteins.

154 Mice lacking all R7-RGS subtypes exhibit diverse neurological phenotypes, an

155 nteraction between activated Galpha13 and R7-RGS heterotrimers, indicating that these effector RhoGEF

156 heterotrimeric complexes with Gbeta5 and R7-RGS-binding protein (R7BP) that regulate G protein-coupl

157 with R7-RGS heterotrimers containing any R7-RGS isoform.

158 R7BP-bound R7-RGS/Gbeta5 complexes and Gbetagamma dimers interact nonc

159 Although each R7-RGS subtype forms heterotrimeric complexes with Gbeta5 a

160 regulator of G protein signaling family (R7-RGS) critically regulates nervous system development and

161 hese effector RhoGEFs can engage Galpha13.R7-RGS complexes.

162 Because Galpha13/R7-RGS interaction required R7BP, we analyzed phenotypes of

163 units, several neurological phenotypes of R7-RGS knock-out mice are not readily explained by dysregul

164 d humans bearing mutations in the retinal R7-RGS isoform RGS9-1 have vision deficits.

165 findings provide the first evidence that R7-RGS heterotrimers interact with Galpha13 to augment sign

166 alpha13 because it had not been linked to R7-RGS complexes before.

167 xpands the diversity of functions whereby R7-RGS complexes regulate critical aspects of nervous syste

168 s active or inactive state interacts with R7-RGS heterotrimers containing any R7-RGS isoform.

169 rch for novel proteins that interact with R7-RGS heterotrimers in the mouse brain.

170 odulation occurs by channel assembly with R7-RGS/Gbeta5 complexes under allosteric control of R7 RGS-

171 We show that GPR158/179 recruited RGS complexes to the plasma membrane and augmented their

172 annel assembly with allosterically regulated RGS protein complexes, which provide a target for modula

173 ta, and Ggamma subunits and their regulatory RGS (Regulator of G-protein Signaling) protein are conse

174 After injury, the complex gradually releases RGS proteins, limiting platelet activation and providing

175 dulation by the G12 and G13 proteins via RH (RGS homology) containing RhoGEFs.

176 RGS-containing RhoGEFs (RGS-RhoGEFs) represent a direct link between the G(12) c

177 nce (NMR) spectroscopy, relaxed grid search (RGS), molecular dynamics (MD) simulations, and quantum m

178 Several RGS proteins have been implicated in the cardiac remodel

179 Several RGS proteins have reduced expression or function in path

180 Because several RGS proteins are rapidly degraded by the N-end rule path

181 Regulators of G-protein signaling (RGS proteins) belong to a diverse protein family that wa

182 known as regulators of G protein signaling (RGS proteins).

183 uption of regulators of G protein signaling (RGS) activity at G(alpha)i2.

184 Regulators of G protein signaling (RGS) are GTPase-activating proteins (GAPs) for G(i) and

185 nd Gbeta5-regulators of G-protein signaling (RGS) complexes.

186 N-terminal regulator of G protein signaling (RGS) domain binds active Galphai/o-GTP, whereas the C-te

187 xin1 has a regulator of G-protein signaling (RGS) domain that binds adenomatous polyposis coli and Ga

188 x (PX) and regulator of G protein signaling (RGS) domains.

189 leiotropic regulator of G protein signaling (RGS) family member RGS6 suppresses Ras-induced cellular

190 The regulator of G protein signaling (RGS) family of proteins serves critical roles in G prote

191 ber of the regulator of G protein signaling (RGS) family, inhibits G protein-coupled receptor signali

192 Regulators of G protein Signaling (RGS) promote deactivation of heterotrimeric G proteins t

193 etics, the regulator of G-protein signaling (RGS) protein family modulates the timing of GIRK activit

194 truncated regulator of G protein signaling (RGS) protein or a Gbetagamma-sequestering domain to a se

195 The regulator of G protein signaling (RGS) protein Sst2 acts by accelerating GTP hydrolysis an

196 of the R7 regulator of G-protein signaling (RGS) protein subfamily are versatile regulators of G-pro

197 The regulators of G protein signaling (RGS) protein superfamily negatively controls G protein-c

198 ility of a regulator of G protein signaling (RGS) protein to suppress noise.

199 s, and the REGULATOR OF G-PROTEIN SIGNALING (RGS) protein.

200 R7 family regulators of G protein signaling (RGS) proteins (RGS6, RGS7, RGS9, and RGS11) instead of G

201 Regulator of G protein signaling (RGS) proteins act to temporally modulate the activity of

202 Regulator of G-protein signaling (RGS) proteins are critical modulators of GPCR activity,

203 Regulators of G protein signaling (RGS) proteins are emerging as potentially important drug

204 The regulator of G-protein signaling (RGS) proteins are key interactors and critical modulator

205 Regulator of G-protein signaling (RGS) proteins are potent inhibitors of heterotrimeric G-

206 Regulators of G protein signaling (RGS) proteins are potent negative modulators of G protei

207 Regulator of G-protein signaling (RGS) proteins classically function as negative modulator

208 Endogenous regulator of G-protein signaling (RGS) proteins have been implicated as key inhibitors of

209 Regulator of G protein signaling (RGS) proteins interact with activated Galpha subunits vi

210 ized that regulators of G protein signaling (RGS) proteins may be involved.

211 izes with regulators of G protein signaling (RGS) proteins of the R7 family instead of Ggamma.

212 Regulators of G protein signaling (RGS) proteins of the R7 subfamily limit signaling by neu

213 Regulator of G protein signaling (RGS) proteins play essential roles in the regulation of

214 ntains two Regulator of G-protein Signaling (RGS) proteins RGS7 and RGS11 that directly act on Go and

215 ence that regulators of G-protein signaling (RGS) proteins serve this role in platelets, using mice w

216 ypothesize Regulator of G-Protein Signaling (RGS) proteins, and specifically RGS5, are endogenous rep

217 family of regulators of G protein signaling (RGS) proteins, comprising RGS6, RGS7, RGS9, and RGS11, r

218 ruits the regulators of G-protein signaling (RGS) proteins, RGS7 and RGS11, to the dendritic tips of

219 ns and the regulator of G-protein signaling (RGS) proteins, which accelerate the inherent GTPase acti

220 Regulator of G protein signaling (RGS) proteins, which function to inactivate G proteins,

221 ped by the regulator of G protein signaling (RGS) proteins, which promote G protein deactivation.

222 eract with regulator of G protein signaling (RGS) proteins.

223 led by the regulator of G-protein signaling (RGS) proteins.

224 led by the regulator of G protein signaling (RGS) proteins.

225 e with the regulator of G protein signaling (RGS) Sst2, a GTPase-activating protein that dampens pher

226 lex of the regulator of G protein signaling (RGS), Gbeta(5)-RGS7, can inhibit signal transduction via

227 studied R7 regulator of G protein signaling (RGS)-binding protein (R7BP), a palmitoylated allosteric

228 t disables regulator of G-protein signaling (RGS)-Galpha(i2) interactions accumulate in the bone marr

229 ) 1 and 2, regulator of G protein signaling (RGS)-homology-RhoGEFs (PDZ domain-containing RhoGEF and

230 tion, and regulators of G protein-signaling (RGS) 4 function in knockout mice.

231 ears ago, regulators of G protein-signaling (RGS) proteins have received considerable attention as po

232 tor of G protein-coupled receptor signaling (RGS) domain that attenuates Galphas-coupled G protein-co

233 amily of "regulator of G protein signaling" (RGS) proteins.

234 ivity of "regulator of G-protein signaling" (RGS) proteins.

235 evidence has revealed key roles for specific RGS proteins in multiple signaling pathways at neuronal

236 highlight the current knowledge of specific RGS proteins (RGS2, RGS4, RGS7, RGS9-2, and RGS14) that

237 ia-associated RhoGEF (LARG), a RhoA-specific RGS-RhoGEF, is required for abscission, the final stage

238 s of SSRIs, but the identity of the specific RGS proteins involved remains unknown.

239 We also show that SPL/RGS/SHP1 complexes are present in resting platelets wher

240 blocks cAMP-induced dissociation of the SPL/RGS/SHP-1 complex.

241 Thus, we propose that the role of the SPL/RGS/SHP1 complex in platelets is time and context depend

242 ering dephosphorylation and decay of the SPL/RGS/SHP1 complex.

243 g G protein and GPCR selectivity of striatal RGS proteins.

244 R7 subfamily RGS proteins are stabilized by the G-protein subunit Gbe

245 directly act on Go and two adaptor subunits: RGS Anchor Protein (R9AP) and the orphan receptor, GPR17

246 er injection) and (99m)Tc-PSMA-I&S-supported RGS (16 h after injection) were performed in 1 PCa patie

247 maging and therapy) for radioguided surgery (RGS) of small metastatic prostate cancer (PCa) soft-tiss

248 A novel radioguided surgery (RGS) technique exploiting beta- radiation has been propo

249 A novel radioguided surgery (RGS) technique for cerebral tumors using beta(-) radiati

250 ior performance as a probe for PSMA-targeted RGS and also hint toward the unexpected potential of (99

251 R7BP targets RGS proteins to the plasma membrane and augments their G

252 seven transmembrane domain and a C-terminal RGS box.

253 d as GEFs and those as GAPs (with C-terminal RGS domains) for Galphas.

254 regulator of Hh-mediated signaling and that RGS proteins are potential targets for novel therapeutic

255 CCG-4986, lack of inhibition indicates that RGS proteins exhibit fundamental differences in their re

256 Strikingly, we observed that RGS activity is augmented by membrane recruitment, in an

257 In this study, we show that RGS protein/Galphai2 interactions are essential for norm

258 Our results show that RGS proteins are widely distributed in the monocot linea

259 thway-selective manner, and (3) suggest that RGS proteins help to prevent unwarranted platelet activa

260 The RGS domain of RGS6, known only for its GTPase-activating

261 ow AtGPA1 is regulated by Gbetagamma and the RGS (regulator of G protein signaling) protein AtRGS1, w

262 tly bound to Gbeta subunit Gbeta(5), and the RGS domain responsible for the interaction with Galpha s

263 communication between the GPR motif and the RGS domain upon G protein binding and examined whether R

264 organization of their sequences flanking the RGS domain, which contain several additional functional

265 rovide evidence of an essential role for the RGS-containing RhoGEF family in signaling to Rho by Galp

266 RGS inhibitors and provides insight into the RGS family members for which drug discovery efforts may

267 hat modification of Cys132, located near the RGS/Galpha interaction surface, modestly inhibits Galpha

268 eraction required the DEP domain but not the RGS and DHEX domains or the Gbeta5 subunit.

269 acts can be maintained between alpha6 of the RGS domain and Switch III of Galphaq, regions of high se

270 e M3R by Gbeta(5)-RGS7 is independent of the RGS domain but requires binding of the DEP domain to the

271 Since RGS4 is a member of the RGS family of proteins that act to reduce the lifetime o

272 GTPase-accelerating protein activity of the RGS protein by using small molecules.

273 liomas (HGGs) and a feasibility study of the RGS technique in these types of tumor.

274 In terms of feasibility of the RGS technique, we estimated that by administering a 3 MB

275 ight into the mechanism of regulation of the RGS-RhoGEF and broadens our understanding of G protein s

276 ntionally, PDZ-RhoGEF (PRG), a member of the RGS-RhoGEFs, binds tightly to both nucleotide-free and a

277 We found that the RGS protein Sst2 limits variability in transcription and

278 stability studies demonstrate binding to the RGS but not to Galpha(o).

279 c site results in significant changes to the RGS interaction surface with Galpha; 2) this identifies

280 modification of cysteine residues within the RGS domain that are located distal to the Galpha-binding

281 ine residues are highly conserved within the RGS family, many of these inhibitors display activity to

282 although slight differences exist within the RGS homology (RH) bundle subdomain, substrate-binding si

283 act with activated Galpha subunits via their RGS domains and accelerate the hydrolysis of GTP.

284 lineate the structural organization of these RGS-PX proteins, revealing a protein family with a modul

285 information on the biological roles of this RGS-containing family of RhoGEFs in vivo.

286 embryonic fibroblasts defective in all three RGS-containing RhoGEFs.

287 , the first biochemical function ascribed to RGS proteins, is sufficient to explain the activation ki

288 to cholinergic stimulation, possibly due to RGS protein downregulation.

289 Animals rendered insensitive to RGS protein regulation through a mutation in G(alpha)i2

290 In neurons of the striatum, two RGS proteins, RGS7 and RGS9-2, regulate signaling by mu-

291 is mammalian SNX19, which lacks the typical RGS structure but preserves all other domains.

292 ignaling pathway used by IL-17 to upregulate RGS.

293 In vitro, RGS proteins have been shown to inhibit signaling by ago

294 When RGS activity is abrogated, septins are partially disorga

295 Despite many investigations, whether RGS proteins modulate GIRK activity in neurons by mechan

296 At present, it remains unknown whether RGS proteins play a role in regulating insulin release.

297 RhoA/Rho kinase has not been associated with RGS molecules.

298 NFR1 interacts with RGS proteins and phosphorylates them.

299 le ligand receptors of bacterial origin with RGS domains and an extraordinary diversity of membrane-l

300 The yeast RGS protein Sst2 is regulated at both the transcriptiona