메뉴 건너뛰기




Volumn 105, Issue 17, 2008, Pages 6457-6462

Structural diversity in the RGS domain and its interaction with heterotrimeric G protein α-subunits

Author keywords

GTPase accelerating proteins; NMR structure; RGS proteins; x ray crystallography

Indexed keywords

HETEROTRIMERIC GUANINE NUCLEOTIDE BINDING PROTEIN; PROTEIN SUBUNIT; RGS PROTEIN; APOPROTEIN; GUANINE NUCLEOTIDE BINDING PROTEIN ALPHA SUBUNIT;

EID: 44049098168     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0801508105     Document Type: Article
Times cited : (157)

References (42)
  • 1
    • 25444482429 scopus 로고    scopus 로고
    • Mammalian G proteins and their cell type specific functions
    • Wettschureck N, Offermanns S (2005) Mammalian G proteins and their cell type specific functions. Physiol Rev 85:1159-1204.
    • (2005) Physiol Rev , vol.85 , pp. 1159-1204
    • Wettschureck, N.1    Offermanns, S.2
  • 3
    • 34547157646 scopus 로고    scopus 로고
    • Receptor-mediated activation of heterotrimeric G-proteins: Current structural insights
    • Johnston CA, Siderovski DP (2007) Receptor-mediated activation of heterotrimeric G-proteins: Current structural insights. Mol Pharmacol 72:219-230.
    • (2007) Mol Pharmacol , vol.72 , pp. 219-230
    • Johnston, C.A.1    Siderovski, D.P.2
  • 5
    • 25444528729 scopus 로고    scopus 로고
    • The GAPs, GEFs, and GDIs of heterotrimeric G-protein alpha subunits
    • Siderovski DP, Willard FS (2005) The GAPs, GEFs, and GDIs of heterotrimeric G-protein alpha subunits. Int J Biol Sci 1:51-66.
    • (2005) Int J Biol Sci , vol.1 , pp. 51-66
    • Siderovski, D.P.1    Willard, F.S.2
  • 6
    • 0030982264 scopus 로고    scopus 로고
    • Structure of RGS4 bound to AlF4-activated G(i alpha1): Stabilization of the transition state for GTP hydrolysis
    • Tesmer JJ, Berman DM, Gilman AG, Sprang SR (1997) Structure of RGS4 bound to AlF4-activated G(i alpha1): Stabilization of the transition state for GTP hydrolysis. Cell 89:251-261.
    • (1997) Cell , vol.89 , pp. 251-261
    • Tesmer, J.J.1    Berman, D.M.2    Gilman, A.G.3    Sprang, S.R.4
  • 7
    • 0030738476 scopus 로고    scopus 로고
    • The regulators of G protein signaling (RGS) domains of RGS4, RGS10, and GAIP retain GTPase activating protein activity in vitro
    • Popov S, Yu K, Kozasa T, Wilkie TM (1997) The regulators of G protein signaling (RGS) domains of RGS4, RGS10, and GAIP retain GTPase activating protein activity in vitro. Proc Natl Acad Sci USA 94:7216-7220.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 7216-7220
    • Popov, S.1    Yu, K.2    Kozasa, T.3    Wilkie, T.M.4
  • 8
    • 0032567439 scopus 로고    scopus 로고
    • The N-terminal domain of RGS4 confers receptor-selective inhibition of G protein signaling
    • Zeng W, et al. (1998) The N-terminal domain of RGS4 confers receptor-selective inhibition of G protein signaling. J Biol Chem 273:34687-34690.
    • (1998) J Biol Chem , vol.273 , pp. 34687-34690
    • Zeng, W.1
  • 9
    • 0032573221 scopus 로고    scopus 로고
    • A G protein γ-subunit-like domain shared between RGS11 and other RGS proteins specifies binding to Gβ5 subunits
    • Snow BE, et al. (1998) A G protein γ-subunit-like domain shared between RGS11 and other RGS proteins specifies binding to Gβ5 subunits. Proc Natl Acad Sci USA 95:13307-13312.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 13307-13312
    • Snow, B.E.1
  • 10
    • 34247274512 scopus 로고    scopus 로고
    • Selective role for RGS12 as a Ras/Raf/MEK scaffold in nerve growth factor-mediated differentiation
    • Willard MD, et al. (2007) Selective role for RGS12 as a Ras/Raf/MEK scaffold in nerve growth factor-mediated differentiation. EMBO J 26:2029-2040.
    • (2007) EMBO J , vol.26 , pp. 2029-2040
    • Willard, M.D.1
  • 12
    • 15544373780 scopus 로고    scopus 로고
    • Structure of the p115RhoGEF rgRGS domain-Galpha13/i1 chimera complex suggests convergent evolution of a GTPase activator
    • Chen Z, Singer WD, Sternweis PC, Sprang SR (2005) Structure of the p115RhoGEF rgRGS domain-Galpha13/i1 chimera complex suggests convergent evolution of a GTPase activator. Nat Struct Mol Biol 12:191-197.
    • (2005) Nat Struct Mol Biol , vol.12 , pp. 191-197
    • Chen, Z.1    Singer, W.D.2    Sternweis, P.C.3    Sprang, S.R.4
  • 13
    • 28844463975 scopus 로고    scopus 로고
    • Snapshot of activated G proteins at the membrane: The Galphaq-GRK2-Gbetagamma complex
    • Tesmer VM, Kawano T, Shankaranarayanan A, Kozasa T, Tesmer JJ (2005) Snapshot of activated G proteins at the membrane: the Galphaq-GRK2-Gbetagamma complex. Science 310:1686-1690.
    • (2005) Science , vol.310 , pp. 1686-1690
    • Tesmer, V.M.1    Kawano, T.2    Shankaranarayanan, A.3    Kozasa, T.4    Tesmer, J.J.5
  • 14
    • 0006078178 scopus 로고    scopus 로고
    • Regulation of T cell activation, anxiety, and male aggression by RGS2
    • Oliveira-Dos-Santos AJ, et al. (2000) Regulation of T cell activation, anxiety, and male aggression by RGS2. Proc Natl Acad Sci USA 97:12272-12277.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 12272-12277
    • Oliveira-Dos-Santos, A.J.1
  • 15
    • 11844254278 scopus 로고    scopus 로고
    • Genetic dissection of a behavioral quantitative trait locus shows that Rgs2 modulates anxiety in mice
    • Yalcin B, et al. (2004) Genetic dissection of a behavioral quantitative trait locus shows that Rgs2 modulates anxiety in mice. Nat Genet 36:1197-1202.
    • (2004) Nat Genet , vol.36 , pp. 1197-1202
    • Yalcin, B.1
  • 16
    • 10744233990 scopus 로고    scopus 로고
    • Regulator of G-protein signaling-2 mediates vascular smooth muscle relaxation and blood pressure
    • Tang KM, et al. (2003) Regulator of G-protein signaling-2 mediates vascular smooth muscle relaxation and blood pressure. Nat Med 9:1506-1512.
    • (2003) Nat Med , vol.9 , pp. 1506-1512
    • Tang, K.M.1
  • 17
    • 0037330249 scopus 로고    scopus 로고
    • Hypertension and prolonged vasoconstrictor signaling in RGS2-deficient mice
    • Heximer SP, et al. (2003) Hypertension and prolonged vasoconstrictor signaling in RGS2-deficient mice. J Clin Invest 111:445-452.
    • (2003) J Clin Invest , vol.111 , pp. 445-452
    • Heximer, S.P.1
  • 19
    • 17344374133 scopus 로고    scopus 로고
    • Dynamic regulation of RGS2 suggests a novel mechanism in G-protein signaling and neuronal plasticity
    • Ingi T, et al. (1998) Dynamic regulation of RGS2 suggests a novel mechanism in G-protein signaling and neuronal plasticity. J Neurosci 18:7178-7188.
    • (1998) J Neurosci , vol.18 , pp. 7178-7188
    • Ingi, T.1
  • 20
    • 0036765564 scopus 로고    scopus 로고
    • Characterization and comparison of RGS2 and RGS4 as GTPase-activating proteins for m2 muscarinic receptor-stimulated G(i)
    • Cladman W, Chidiac P (2002) Characterization and comparison of RGS2 and RGS4 as GTPase-activating proteins for m2 muscarinic receptor-stimulated G(i). Mol Pharmacol 62:654-659.
    • (2002) Mol Pharmacol , vol.62 , pp. 654-659
    • Cladman, W.1    Chidiac, P.2
  • 21
    • 0035931919 scopus 로고    scopus 로고
    • Structural determinants for regulation of phosphodiesterase by a G protein at 2.0 A
    • Slep KC, et al. (2001) Structural determinants for regulation of phosphodiesterase by a G protein at 2.0 A. Nature 409:1071-1077.
    • (2001) Nature , vol.409 , pp. 1071-1077
    • Slep, K.C.1
  • 22
    • 44049099132 scopus 로고    scopus 로고
    • Molecular architecture of G-α-o and the structural basis for RGS16-mediated deactivation
    • Slep KC, et al. (2008) Molecular architecture of G-α-o and the structural basis for RGS16-mediated deactivation. Proc Natl Acad Sci USA 105:6243-6248.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 6243-6248
    • Slep, K.C.1
  • 23
    • 0036490096 scopus 로고    scopus 로고
    • Regulators of G-protein signalling as new central nervous system drug targets
    • Neubig RR, Siderovski DP (2002) Regulators of G-protein signalling as new central nervous system drug targets. Nat Rev Drug Discov 1:187-197.
    • (2002) Nat Rev Drug Discov , vol.1 , pp. 187-197
    • Neubig, R.R.1    Siderovski, D.P.2
  • 24
    • 0032475518 scopus 로고    scopus 로고
    • RGSZ1, a Gz-selective regulator of G protein signaling whose action is sensitive to the phosphorylation state of Gzalpha
    • Glick JL, Meigs TE, Miron A, Casey PJ (1998) RGSZ1, a Gz-selective regulator of G protein signaling whose action is sensitive to the phosphorylation state of Gzalpha. J Biol Chem 273:26008-26013.
    • (1998) J Biol Chem , vol.273 , pp. 26008-26013
    • Glick, J.L.1    Meigs, T.E.2    Miron, A.3    Casey, P.J.4
  • 25
    • 0032475515 scopus 로고    scopus 로고
    • RGSZ1, a Gz-selective RGS protein in brain. Structure, membrane association, regulation by Galphaz phosphorylation, and relationship to a Gz gtpase-activating protein subfamily
    • Wang J, et al. (1998) RGSZ1, a Gz-selective RGS protein in brain. Structure, membrane association, regulation by Galphaz phosphorylation, and relationship to a Gz gtpase-activating protein subfamily. J Biol Chem 273:26014-26025.
    • (1998) J Biol Chem , vol.273 , pp. 26014-26025
    • Wang, J.1
  • 26
    • 0037073785 scopus 로고    scopus 로고
    • Regulator of G protein signaling Z1 (RGSZ1) interacts with Galpha i subunits and regulates Galpha i-mediated cell signaling
    • Wang Y, et al. (2002) Regulator of G protein signaling Z1 (RGSZ1) interacts with Galpha i subunits and regulates Galpha i-mediated cell signaling. J Biol Chem 277:48325-48332.
    • (2002) J Biol Chem , vol.277 , pp. 48325-48332
    • Wang, Y.1
  • 27
    • 0033609905 scopus 로고    scopus 로고
    • Solution structure of human GAIP (Galpha interacting protein): A regulator of G protein signaling
    • de Alba E, De Vries L, Farquhar MG, Tjandra N (1999) Solution structure of human GAIP (Galpha interacting protein): A regulator of G protein signaling. J Mol Biol 291:927-939.
    • (1999) J Mol Biol , vol.291 , pp. 927-939
    • de Alba, E.1    De Vries, L.2    Farquhar, M.G.3    Tjandra, N.4
  • 28
    • 0034691314 scopus 로고    scopus 로고
    • NMR structure of free RGS4 reveals an induced conformational change upon binding Galpha
    • Moy FJ, et al. (2000) NMR structure of free RGS4 reveals an induced conformational change upon binding Galpha. Biochemistry 39:7063-7073.
    • (2000) Biochemistry , vol.39 , pp. 7063-7073
    • Moy, F.J.1
  • 29
    • 0033607789 scopus 로고    scopus 로고
    • G protein selectivity is a determinant of RGS2 function
    • Heximer SP, et al. (1999) G protein selectivity is a determinant of RGS2 function. J Biol Chem 274:34253-34259.
    • (1999) J Biol Chem , vol.274 , pp. 34253-34259
    • Heximer, S.P.1
  • 30
    • 35448929112 scopus 로고    scopus 로고
    • A large data set comparison of protein structures determined by crystallography and NMR: Statistical test for structural differences and the effect of crystal packing
    • Andrec M, et al. (2007) A large data set comparison of protein structures determined by crystallography and NMR: Statistical test for structural differences and the effect of crystal packing. Proteins 69:449-465.
    • (2007) Proteins , vol.69 , pp. 449-465
    • Andrec, M.1
  • 31
    • 2342441008 scopus 로고    scopus 로고
    • + channel
    • + channel. J Biol Chem 279:17260-17268.
    • (2004) J Biol Chem , vol.279 , pp. 17260-17268
    • Ivanina, T.1
  • 33
    • 0030302494 scopus 로고    scopus 로고
    • Dopamine D2L receptor couples to G alpha i2 and G alpha i3 but not G alpha i1, leading to the inhibition of adenylate cyclase in transfected cell lines
    • O'Hara CM, Tang L, Taussig R, Todd RD, O'Malley KL (1996) Dopamine D2L receptor couples to G alpha i2 and G alpha i3 but not G alpha i1, leading to the inhibition of adenylate cyclase in transfected cell lines. J Pharmacol Exp Ther 278:354-360.
    • (1996) J Pharmacol Exp Ther , vol.278 , pp. 354-360
    • O'Hara, C.M.1    Tang, L.2    Taussig, R.3    Todd, R.D.4    O'Malley, K.L.5
  • 34
    • 15644373915 scopus 로고    scopus 로고
    • GTPase activating specificity of RGS12 and binding specificity of an alternatively spliced PDZ (PSD-95/Dlg/ZO-1) domain
    • Snow BE, et al. (1998) GTPase activating specificity of RGS12 and binding specificity of an alternatively spliced PDZ (PSD-95/Dlg/ZO-1) domain. J Biol Chem 273:17749-17755.
    • (1998) J Biol Chem , vol.273 , pp. 17749-17755
    • Snow, B.E.1
  • 35
    • 0033851787 scopus 로고    scopus 로고
    • RGS14, a GTPase-activating protein for Gialpha, attenuates Gialpha- and G13alpha-mediated signaling pathways
    • Cho H, Kozasa T, Takekoshi K, De Gunzburg J, Kehrl JH (2000) RGS14, a GTPase-activating protein for Gialpha, attenuates Gialpha- and G13alpha-mediated signaling pathways. Mol Pharmacol 58:569-576.
    • (2000) Mol Pharmacol , vol.58 , pp. 569-576
    • Cho, H.1    Kozasa, T.2    Takekoshi, K.3    De Gunzburg, J.4    Kehrl, J.H.5
  • 36
    • 0033605581 scopus 로고    scopus 로고
    • The alpha-helical domain of Galphat determines specific interaction with regulator of G protein signaling 9
    • Skiba NP, Yang CS, Huang T, Bae H, Hamm HE (1999) The alpha-helical domain of Galphat determines specific interaction with regulator of G protein signaling 9. J Biol Chem 274:8770-8778.
    • (1999) J Biol Chem , vol.274 , pp. 8770-8778
    • Skiba, N.P.1    Yang, C.S.2    Huang, T.3    Bae, H.4    Hamm, H.E.5
  • 37
    • 33749012581 scopus 로고    scopus 로고
    • Minimal determinants for binding activated G alpha from the structure of a G alpha(i1)-peptide dimer
    • Johnston CA, et al. (2006) Minimal determinants for binding activated G alpha from the structure of a G alpha(i1)-peptide dimer. Biochemistry 45:11390-11400.
    • (2006) Biochemistry , vol.45 , pp. 11390-11400
    • Johnston, C.A.1
  • 38
    • 34548289765 scopus 로고    scopus 로고
    • The RGS protein inhibitor CCG-4986 is a covalent modifier of the RGS4 Galpha-interaction face
    • Kimple AJ, et al. (2007) The RGS protein inhibitor CCG-4986 is a covalent modifier of the RGS4 Galpha-interaction face. Biochim Biophys Acta 1774:1213-1220.
    • (2007) Biochim Biophys Acta , vol.1774 , pp. 1213-1220
    • Kimple, A.J.1
  • 39
    • 33845764737 scopus 로고    scopus 로고
    • Differential G-alpha interaction capacities of the GoLoco motifs in Rap GTPase activating proteins
    • Willard FS, Low AB, McCudden CR, Siderovski DP (2007) Differential G-alpha interaction capacities of the GoLoco motifs in Rap GTPase activating proteins. Cell Signal 19:428-438.
    • (2007) Cell Signal , vol.19 , pp. 428-438
    • Willard, F.S.1    Low, A.B.2    McCudden, C.R.3    Siderovski, D.P.4
  • 40
    • 35748983198 scopus 로고    scopus 로고
    • G{alpha}q directly activates p63RhoGEF and Trio via a conserved extension of the Dbl homology-associated pleckstrin homology domain
    • Rojas RJ, et al. (2007) G{alpha}q directly activates p63RhoGEF and Trio via a conserved extension of the Dbl homology-associated pleckstrin homology domain. J Biol Chem 282:29201-29210.
    • (2007) J Biol Chem , vol.282 , pp. 29201-29210
    • Rojas, R.J.1
  • 41
    • 33646351018 scopus 로고    scopus 로고
    • Covalent immobilization of histidine-tagged proteins for surface plasmon resonance
    • Willard FS, Siderovski DP (2006) Covalent immobilization of histidine-tagged proteins for surface plasmon resonance. Anal Biochem 353:147-149.
    • (2006) Anal Biochem , vol.353 , pp. 147-149
    • Willard, F.S.1    Siderovski, D.P.2
  • 42
    • 33947544164 scopus 로고    scopus 로고
    • RGS proteins: Swiss army knives in seven-transmembrane domain receptor signaling networks
    • Heximer SP, Blumer KJ (2007) RGS proteins: Swiss army knives in seven-transmembrane domain receptor signaling networks. Sci STKE 2007, pe2.
    • (2007) Sci STKE 2007, pe2
    • Heximer, S.P.1    Blumer, K.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.