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Volumn 17, Issue 1, 2009, Pages 42-54

Functions and regulatory mechanisms of Gq-signaling pathways

Author keywords

Differentiation; Flotillin; Gq; Interacting proteins; Migration; Neural progenitor cells; Pasteurella multocida toxin; Phospholipase C ; Proliferation; Ric 8; YM 254890

Indexed keywords

BACTERIAL TOXIN; CHOLERA TOXIN; ENDOTHELIN; ENZYME INHIBITOR; GUANINE NUCLEOTIDE BINDING PROTEIN ALPHA SUBUNIT; GUANINE NUCLEOTIDE EXCHANGE FACTOR; GUANOSINE TRIPHOSPHATASE; HYPOPHYSIS ADENYLATE CYCLASE ACTIVATING POLYPEPTIDE; PASTEURELLA MULTOCIDA TOXIN; PERTUSSIS TOXIN; PHOSPHOLIPASE C BETA; RHOA GUANINE NUCLEOTIDE BINDING PROTEIN; SCAFFOLD PROTEIN; UNCLASSIFIED DRUG; YM 254890;

EID: 60149088035     PISSN: 1424862X     EISSN: None     Source Type: Journal    
DOI: 10.1159/000186689     Document Type: Review
Times cited : (126)

References (129)
  • 1
    • 0023062991 scopus 로고
    • G proteins: Transducers of receptor-generated signals
    • Gilman AG: G proteins: transducers of receptor-generated signals. Annu Rev Biochem 1987;56:614-649.
    • (1987) Annu Rev Biochem , vol.56 , pp. 614-649
    • Gilman, A.G.1
  • 2
  • 3
    • 0025834532 scopus 로고
    • Diversity of G proteins in signal transduction
    • Simon MI, Strathmann MP, Gautam N: Diversity of G proteins in signal transduction. Science 1991;252:802-808.
    • (1991) Science , vol.252 , pp. 802-808
    • Simon, M.I.1    Strathmann, M.P.2    Gautam, N.3
  • 4
    • 37549016836 scopus 로고    scopus 로고
    • Heterotrimeric G protein activation by G-protein-coupled receptors
    • Oldham WM, Hamm HE: Heterotrimeric G protein activation by G-protein-coupled receptors. Nat Rev Mol Cell Biol 2008;9:67-93.
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 67-93
    • Oldham, W.M.1    Hamm, H.E.2
  • 5
    • 0034927336 scopus 로고    scopus 로고
    • Regulation of phosphoinositide-specific phospholipase C
    • Rhee SG: Regulation of phosphoinositide-specific phospholipase C. Annu Rev Biochem 2001;70:281-312.
    • (2001) Annu Rev Biochem , vol.70 , pp. 281-312
    • Rhee, S.G.1
  • 6
    • 0027050601 scopus 로고
    • Activation of phospholipase C by α1-adrenergic receptors is mediated by the α subunits of Gq family
    • Wu D, Katz A, Lee CH, Simon MI: Activation of phospholipase C by α1-adrenergic receptors is mediated by the α subunits of Gq family. J Biol Chem 1992;267:25798-25802.
    • (1992) J Biol Chem , vol.267 , pp. 25798-25802
    • Wu, D.1    Katz, A.2    Lee, C.H.3    Simon, M.I.4
  • 7
    • 0027214868 scopus 로고
    • Regulation of purified subtypes of phosphatidylinositol-specific phospholipase C β by G protein α and β γ subunits
    • Smrcka AV, Sternweis PC: Regulation of purified subtypes of phosphatidylinositol-specific phospholipase C β by G protein α and β γ subunits. J Biol Chem 1993;268:9667-9674.
    • (1993) J Biol Chem , vol.268 , pp. 9667-9674
    • Smrcka, A.V.1    Sternweis, P.C.2
  • 8
    • 0027167915 scopus 로고
    • Purification from Sf9 cells and characterization of recombinant Gqα and G11α. Activation of purified phospholipase C isozymes by Gα subunits
    • Hepler JR, Kozasa T, Smrcka AV, Simon MI, Rhee SG, Sternweis PC, Gilman AG: Purification from Sf9 cells and characterization of recombinant Gqα and G11α. Activation of purified phospholipase C isozymes by Gα subunits. J Biol Chem 1993;268:14367-14375.
    • (1993) J Biol Chem , vol.268 , pp. 14367-14375
    • Hepler, J.R.1    Kozasa, T.2    Smrcka, A.V.3    Simon, M.I.4    Rhee, S.G.5    Sternweis, P.C.6    Gilman, A.G.7
  • 9
    • 0028283331 scopus 로고
    • Activation of phospholipase C β4 by heterotrimeric GTP-binding proteins
    • Jiang H, Wu D, Simon MI: Activation of phospholipase C β4 by heterotrimeric GTP-binding proteins. J Biol Chem 1994;269:7593-7596.
    • (1994) J Biol Chem , vol.269 , pp. 7593-7596
    • Jiang, H.1    Wu, D.2    Simon, M.I.3
  • 10
    • 0027489221 scopus 로고
    • Purification and characterization of recombinant G16α from Sf9 cells: Activation of purified phospholipase C isozymes by G-protein α subunits
    • Kozasa T, Hepler JR, Smrcka AV, Simon MI, Rhee SG, Sternweis PC, Gilman AG: Purification and characterization of recombinant G16α from Sf9 cells: activation of purified phospholipase C isozymes by G-protein α subunits. Proc Natl Acad Sci USA 1993;90:9176-9180.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 9176-9180
    • Kozasa, T.1    Hepler, J.R.2    Smrcka, A.V.3    Simon, M.I.4    Rhee, S.G.5    Sternweis, P.C.6    Gilman, A.G.7
  • 11
    • 0029670037 scopus 로고    scopus 로고
    • Identification of determinants in the α-subunit of Gq required for phospholipase C activation
    • Venkatakrishnan G, Exton JH: Identification of determinants in the α-subunit of Gq required for phospholipase C activation. J Biol Chem 1996;271:5066-5072.
    • (1996) J Biol Chem , vol.271 , pp. 5066-5072
    • Venkatakrishnan, G.1    Exton, J.H.2
  • 12
    • 0027537482 scopus 로고
    • Removal of the carboxyl-terminal region of phospholipase C-β1 by calpain abolishes activation by Gαq
    • Park D, Jhon DY, Lee CW, Ryu SH, Rhee SG: Removal of the carboxyl-terminal region of phospholipase C-β1 by calpain abolishes activation by Gαq. J Biol Chem 1993;268:3710-3714.
    • (1993) J Biol Chem , vol.268 , pp. 3710-3714
    • Park, D.1    Jhon, D.Y.2    Lee, C.W.3    Ryu, S.H.4    Rhee, S.G.5
  • 13
    • 0029841118 scopus 로고    scopus 로고
    • The role of carboxyl-terminal basic amino acids in Gqα-dependent activation, particulate association, and nuclear localization of phospholipase C-β1
    • Kim CG, Park D, Rhee SG: The role of carboxyl-terminal basic amino acids in Gqα-dependent activation, particulate association, and nuclear localization of phospholipase C-β1. J Biol Chem 1996;271:21187-21192.
    • (1996) J Biol Chem , vol.271 , pp. 21187-21192
    • Kim, C.G.1    Park, D.2    Rhee, S.G.3
  • 14
    • 0033529292 scopus 로고    scopus 로고
    • Selective interaction of the C2 domains of phospholipase C-β1 and -β2 with activated Gαq subunits: An alternative function for C2-signaling modules
    • Wang T, Pentyala S, Elliott JT, Dowal L, Gupta E, Rebecchi MJ, Scarlata S: Selective interaction of the C2 domains of phospholipase C-β1 and -β2 with activated Gαq subunits: an alternative function for C2-signaling modules. Proc Natl Acad Sci USA 1999;96:7843-7846.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 7843-7846
    • Wang, T.1    Pentyala, S.2    Elliott, J.T.3    Dowal, L.4    Gupta, E.5    Rebecchi, M.J.6    Scarlata, S.7
  • 15
    • 0029961069 scopus 로고    scopus 로고
    • Regulation of phospholipase C-β1 by Gq and m1 muscarinic cholinergic receptor. Steady-state balance of receptor-mediated activation and GTPase-activating protein-promoted deactivation
    • Biddlecome GH, Berstein G, Ross EM: Regulation of phospholipase C-β1 by Gq and m1 muscarinic cholinergic receptor. Steady-state balance of receptor-mediated activation and GTPase-activating protein-promoted deactivation. J Biol Chem 1996;271:7999-8007.
    • (1996) J Biol Chem , vol.271 , pp. 7999-8007
    • Biddlecome, G.H.1    Berstein, G.2    Ross, E.M.3
  • 16
    • 0033538337 scopus 로고    scopus 로고
    • Phospholipase C-β1 directly accelerates GTP hydrolysis by Gαq and acceleration is inhibited by βγ subunits
    • Chidiac P, Ross EM: Phospholipase C-β1 directly accelerates GTP hydrolysis by Gαq and acceleration is inhibited by βγ subunits. J Biol Chem 1999;274:19639-19643.
    • (1999) J Biol Chem , vol.274 , pp. 19639-19643
    • Chidiac, P.1    Ross, E.M.2
  • 17
    • 0029864554 scopus 로고    scopus 로고
    • Carboxyl-terminal fragments of phospholipase C-β1 with intrinsic Gq GTPase-activating protein (GAP) activity
    • Paulssen RH, Woodson J, Liu Z, Ross EM: Carboxyl-terminal fragments of phospholipase C-β1 with intrinsic Gq GTPase-activating protein (GAP) activity. J Biol Chem 1996;271:26622-26629.
    • (1996) J Biol Chem , vol.271 , pp. 26622-26629
    • Paulssen, R.H.1    Woodson, J.2    Liu, Z.3    Ross, E.M.4
  • 18
    • 25444528729 scopus 로고    scopus 로고
    • The GAPs, GEFs, and GDIs of heterotrimeric G-protein α subunits
    • Siderovski DP, Willard FS: The GAPs, GEFs, and GDIs of heterotrimeric G-protein α subunits. Int J Biol Sci 2005;1:51-66.
    • (2005) Int J Biol Sci , vol.1 , pp. 51-66
    • Siderovski, D.P.1    Willard, F.S.2
  • 19
    • 0036733358 scopus 로고    scopus 로고
    • Cellular regulation of RGS proteins: Modulators and integrators of G protein signaling
    • Hollinger S, Hepler JR: Cellular regulation of RGS proteins: modulators and integrators of G protein signaling. Pharmacol Rev 2002;54:527-559.
    • (2002) Pharmacol Rev , vol.54 , pp. 527-559
    • Hollinger, S.1    Hepler, J.R.2
  • 20
    • 0030610240 scopus 로고    scopus 로고
    • Attenuation of Gi- and Gq-mediated signaling by expression of RGS4 or GAIP in mammalian cells
    • Huang C, Hepler JR, Gilman AG, Mumby SM: Attenuation of Gi- and Gq-mediated signaling by expression of RGS4 or GAIP in mammalian cells. Proc Natl Acad Sci USA 1997;94:6159-6163.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 6159-6163
    • Huang, C.1    Hepler, J.R.2    Gilman, A.G.3    Mumby, S.M.4
  • 21
    • 0030611749 scopus 로고    scopus 로고
    • RGS4 inhibits Gq-mediated activation of mitogen-activated protein kinase and phosphoinositide synthesis
    • Yan Y, Chi PP, Bourne HR: RGS4 inhibits Gq-mediated activation of mitogen-activated protein kinase and phosphoinositide synthesis. J Biol Chem 1997;272:11924-11927.
    • (1997) J Biol Chem , vol.272 , pp. 11924-11927
    • Yan, Y.1    Chi, P.P.2    Bourne, H.R.3
  • 23
    • 0031053536 scopus 로고    scopus 로고
    • Potential role for a regulator of G protein signaling (RGS3) in gonadotropin-releasing hormone-stimulated desensitization
    • Neill JD, Duck LW, Sellers JC, Musgrove LC, Scheschonka A, Druey KM, Kehrl JH: Potential role for a regulator of G protein signaling (RGS3) in gonadotropin-releasing hormone-stimulated desensitization. Endocrinology 1997;138:843-846.
    • (1997) Endocrinology , vol.138 , pp. 843-846
    • Neill, J.D.1    Duck, L.W.2    Sellers, J.C.3    Musgrove, L.C.4    Scheschonka, A.5    Druey, K.M.6    Kehrl, J.H.7
  • 24
    • 0037162557 scopus 로고    scopus 로고
    • Alternative splicing of RGS8 gene determines inhibitory function of receptor type-specific Gq signaling
    • Saitoh O, Murata Y, Odagiri M, Itoh M, Itoh H, Misaka T, Kubo Y: Alternative splicing of RGS8 gene determines inhibitory function of receptor type-specific Gq signaling. Proc Natl Acad Sci USA 2002;99:10138-10143.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 10138-10143
    • Saitoh, O.1    Murata, Y.2    Odagiri, M.3    Itoh, M.4    Itoh, H.5    Misaka, T.6    Kubo, Y.7
  • 25
    • 0033104788 scopus 로고    scopus 로고
    • Regulators of G protein signaling exhibit distinct patterns of gene expression and target G protein specificity in human lymphocytes
    • Beadling C, Druey, KM, Richter G, Kehrl JH, Smith KA: Regulators of G protein signaling exhibit distinct patterns of gene expression and target G protein specificity in human lymphocytes. J Immunol 1999;162:2677-2682.
    • (1999) J Immunol , vol.162 , pp. 2677-2682
    • Beadling, C.1    Druey, K.M.2    Richter, G.3    Kehrl, J.H.4    Smith, K.A.5
  • 28
    • 0037053368 scopus 로고    scopus 로고
    • Functional characterization of the G protein regulator RGS13
    • Johnson EN, Druey KM: Functional characterization of the G protein regulator RGS13. J Biol Chem 2002;277:16768-16774.
    • (2002) J Biol Chem , vol.277 , pp. 16768-16774
    • Johnson, E.N.1    Druey, K.M.2
  • 29
    • 0030029727 scopus 로고    scopus 로고
    • Inhibition of G-protein-mediated MAP kinase activation by a new mammalian gene family
    • Druey KM, Blumer KJ, Kang VH, Kehrl JH: Inhibition of G-protein-mediated MAP kinase activation by a new mammalian gene family. Nature 1996;379:742-746.
    • (1996) Nature , vol.379 , pp. 742-746
    • Druey, K.M.1    Blumer, K.J.2    Kang, V.H.3    Kehrl, J.H.4
  • 30
    • 0035720794 scopus 로고    scopus 로고
    • Measuring RGS protein interactions with Gqα
    • Chidiac P, Gadd ME, Hepler JR: Measuring RGS protein interactions with Gqα. Methods Enzymol 2002;344:686-702.
    • (2002) Methods Enzymol , vol.344 , pp. 686-702
    • Chidiac, P.1    Gadd, M.E.2    Hepler, J.R.3
  • 32
    • 0031017573 scopus 로고    scopus 로고
    • RGS4 and GAIP are GTPase-activating proteins for Gqα and block activation of phospholipase Cβ by γ-thio-GTP-Gqα
    • Hepler JR, Berman DM, Gilman AG, Kozasa T: RGS4 and GAIP are GTPase-activating proteins for Gqα and block activation of phospholipase Cβ by γ-thio-GTP-Gqα. Proc Natl Acad Sci USA 1997;94:428-432.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 428-432
    • Hepler, J.R.1    Berman, D.M.2    Gilman, A.G.3    Kozasa, T.4
  • 33
    • 0033798792 scopus 로고    scopus 로고
    • RGS3 is a GTPase-activating protein for Giα and Gqα and a potent inhibitor of signaling by GTPase-deficient forms of Gqα and G11α
    • Scheschonka A, Dessauer CW, Sinnarajah S, Chidiac P, Shi CS, Kehrl JH: RGS3 is a GTPase-activating protein for Giα and Gqα and a potent inhibitor of signaling by GTPase-deficient forms of Gqα and G11α. Mol Pharmacol 2000;58:719-728.
    • (2000) Mol Pharmacol , vol.58 , pp. 719-728
    • Scheschonka, A.1    Dessauer, C.W.2    Sinnarajah, S.3    Chidiac, P.4    Shi, C.S.5    Kehrl, J.H.6
  • 34
    • 0035874503 scopus 로고    scopus 로고
    • A novel regulator of G-protein signaling bearing GAP activity for Gαi and Gαq in megakaryocytes
    • Nagata Y, Oda M, Nakata H, Shozaki Y, Kozasa T, Todokoro K: A novel regulator of G-protein signaling bearing GAP activity for Gαi and Gαq in megakaryocytes. Blood 2001;97:3051-3060.
    • (2001) Blood , vol.97 , pp. 3051-3060
    • Nagata, Y.1    Oda, M.2    Nakata, H.3    Shozaki, Y.4    Kozasa, T.5    Todokoro, K.6
  • 36
    • 0036191304 scopus 로고    scopus 로고
    • Rho GTPases in transformation and metastasis
    • Jaffe AB, Hall A: Rho GTPases in transformation and metastasis. Adv Cancer Res 2002;84:57-80.
    • (2002) Adv Cancer Res , vol.84 , pp. 57-80
    • Jaffe, A.B.1    Hall, A.2
  • 37
    • 33748994545 scopus 로고    scopus 로고
    • Rho GTPases and actin dynamics in membrane protrusions and vesicle trafficking
    • Ridley AJ: Rho GTPases and actin dynamics in membrane protrusions and vesicle trafficking. Trends Cell Biol 2006;16:522-529.
    • (2006) Trends Cell Biol , vol.16 , pp. 522-529
    • Ridley, A.J.1
  • 38
    • 13444252631 scopus 로고    scopus 로고
    • GEF means go: Turning on RHO GTPases with guanine nucleotide-exchange factors
    • Rossman KL, Der CJ, Sondek J: GEF means go: turning on RHO GTPases with guanine nucleotide-exchange factors. Nat Rev Mol Cell Biol 2005;6:167-180.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 167-180
    • Rossman, K.L.1    CJ, D.2    Sondek, J.3
  • 39
    • 0036644975 scopus 로고    scopus 로고
    • Guanine nucleotide exchange factors for Rho GTPases: Turning on the switch
    • Schmidt A, Hall A: Guanine nucleotide exchange factors for Rho GTPases: turning on the switch. Genes Dev 2002;16:1587-1609.
    • (2002) Genes Dev , vol.16 , pp. 1587-1609
    • Schmidt, A.1    Hall, A.2
  • 42
    • 0033605294 scopus 로고    scopus 로고
    • A novel PDZ domain containing guanine nucleotide exchange factor links heterotrimeric G proteins to Rho
    • Fukuhara S, Murga C, Zohar M, Igishi T, Gutkind JS: A novel PDZ domain containing guanine nucleotide exchange factor links heterotrimeric G proteins to Rho. J Biol Chem 1999;274:5868-5879.
    • (1999) J Biol Chem , vol.274 , pp. 5868-5879
    • Fukuhara, S.1    Murga, C.2    Zohar, M.3    Igishi, T.4    Gutkind, J.S.5
  • 43
    • 0037457789 scopus 로고    scopus 로고
    • Gα12 activates Rho GTPase through tyrosine-phosphorylated leukemia-associated RhoGEF
    • Suzuki N, Nakamura S, Mano H, Kozasa T: Gα12 activates Rho GTPase through tyrosine-phosphorylated leukemia-associated RhoGEF. Proc Natl Acad Sci USA 2003;100:733-738.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 733-738
    • Suzuki, N.1    Nakamura, S.2    Mano, H.3    Kozasa, T.4
  • 44
    • 15744364175 scopus 로고    scopus 로고
    • The guanine nucleotide exchange factor p63RhoGEF, a specific link between Gq/11-coupled receptor signaling and RhoA
    • Lutz S, Freichel-Blomquist A, Yang Y, Rümenapp U, Jakobs KH, Schmidt M, Wieland T: The guanine nucleotide exchange factor p63RhoGEF, a specific link between Gq/11-coupled receptor signaling and RhoA. J Biol Chem 2005;280:11134-11139.
    • (2005) J Biol Chem , vol.280 , pp. 11134-11139
    • Lutz, S.1    Freichel-Blomquist, A.2    Yang, Y.3    Rümenapp, U.4    Jakobs, K.H.5    Schmidt, M.6    Wieland, T.7
  • 46
    • 35748983198 scopus 로고    scopus 로고
    • Gαq directly activates p63RhoGEF and Trio via a conserved extension of the Dbl homology-associated pleckstrin homology domain
    • Rojas RJ, Yohe ME, Gershburg S, Kawano T, Kozasa T, Sondek J: Gαq directly activates p63RhoGEF and Trio via a conserved extension of the Dbl homology-associated pleckstrin homology domain. J Biol Chem 2007;282:29201- 29210.
    • (2007) J Biol Chem , vol.282 , pp. 29201-29210
    • Rojas, R.J.1    Yohe, M.E.2    Gershburg, S.3    Kawano, T.4    Kozasa, T.5    Sondek, J.6
  • 48
    • 0033695192 scopus 로고    scopus 로고
    • RIC-8 (Synembryn): A novel conserved protein that is required for Gqα signaling in the C. elegans nervous system
    • Miller KG, Emerson MD, McManus JR, Rand JB: RIC-8 (Synembryn): a novel conserved protein that is required for Gqα signaling in the C. elegans nervous system. Neuron 2000;27:289-299.
    • (2000) Neuron , vol.27 , pp. 289-299
    • Miller, K.G.1    Emerson, M.D.2    McManus, J.R.3    Rand, J.B.4
  • 49
    • 0034533704 scopus 로고    scopus 로고
    • A role for RIC-8 (Synembryn) and GOA-1 (G(o)α) in regulating a subset of centrosome movements during early embryogenesis in Caenorhabditis elegans
    • Miller KG, Rand JB: A role for RIC-8 (Synembryn) and GOA-1 (G(o)α) in regulating a subset of centrosome movements during early embryogenesis in Caenorhabditis elegans. Genetics 2000;156:1649-1660.
    • (2000) Genetics , vol.156 , pp. 1649-1660
    • Miller, K.G.1    Rand, J.B.2
  • 51
    • 6944256893 scopus 로고    scopus 로고
    • Control of embryonic spindle positioning and Gα activity by C. elegans RIC-8
    • Couwenbergs C, Spilker AC, Gotta M: Control of embryonic spindle positioning and Gα activity by C. elegans RIC-8. Curr Biol 2004;14:1871-1876.
    • (2004) Curr Biol , vol.14 , pp. 1871-1876
    • Couwenbergs, C.1    Spilker, A.C.2    Gotta, M.3
  • 52
    • 27844524595 scopus 로고    scopus 로고
    • Drosophila Ric-8 regulates Gαi cortical localization to promote Gαi-dependent planar orientation of the mitotic spindle during asymmetric cell division
    • David NB, Martin CA, Segalen M, Rosenfeld F, Schweisguth F, Bellaïche Y: Drosophila Ric-8 regulates Gαi cortical localization to promote Gαi-dependent planar orientation of the mitotic spindle during asymmetric cell division. Nat Cell Biol 2005;7:1083-1090.
    • (2005) Nat Cell Biol , vol.7 , pp. 1083-1090
    • David, N.B.1    Martin, C.A.2    Segalen, M.3    Rosenfeld, F.4    Schweisguth, F.5    Bellaïche, Y.6
  • 53
    • 28844481199 scopus 로고    scopus 로고
    • Drosophila Ric-8 is essential for plasma-membrane localization of heterotrimeric G proteins
    • Hampoelz B, Hoeller O, Bowman SK, Dunican D, Knoblich JA: Drosophila Ric-8 is essential for plasma-membrane localization of heterotrimeric G proteins. Nat Cell Biol 2005;7:1099-1105.
    • (2005) Nat Cell Biol , vol.7 , pp. 1099-1105
    • Hampoelz, B.1    Hoeller, O.2    Bowman, S.K.3    Dunican, D.4    Knoblich, J.A.5
  • 54
    • 28844482414 scopus 로고    scopus 로고
    • Ric-8 controls Drosophila neural progenitor asymmetric division by regulating heterotrimeric G proteins
    • Wang H, Ng KH, Qian H, Siderovski DP, Chia W, Yu F: Ric-8 controls Drosophila neural progenitor asymmetric division by regulating heterotrimeric G proteins. Nat Cell Biol 2005;7:1091-1098.
    • (2005) Nat Cell Biol , vol.7 , pp. 1091-1098
    • Wang, H.1    Ng, K.H.2    Qian, H.3    Siderovski, D.P.4    Chia, W.5    Yu, F.6
  • 55
    • 0037424298 scopus 로고    scopus 로고
    • Mammalian Ric-8A (synembryn) is a heterotrimeric Gα protein guanine nucleotide exchange factor
    • Tall GG, Krumins AM, Gilman AG: Mammalian Ric-8A (synembryn) is a heterotrimeric Gα protein guanine nucleotide exchange factor. J Biol Chem 2003;278:8356-8362.
    • (2003) J Biol Chem , vol.278 , pp. 8356-8362
    • Tall, G.G.1    Krumins, A.M.2    Gilman, A.G.3
  • 56
    • 0042285767 scopus 로고    scopus 로고
    • Expression of ric-8 (synembryn) gene in the nervous system of developing and adult mouse
    • Tõnissoo T, Meier R, Talts K, Plaas M, Karis A: Expression of ric-8 (synembryn) gene in the nervous system of developing and adult mouse. Gene Expr Patterns 2003;3:591-594.
    • (2003) Gene Expr Patterns , vol.3 , pp. 591-594
    • Tõnissoo, T.1    Meier, R.2    Talts, K.3    Plaas, M.4    Karis, A.5
  • 57
    • 33645830270 scopus 로고    scopus 로고
    • Ric-8A potentiates Gq-mediated signal transduction by acting downstream of G protein-coupled receptor in intact cells
    • Nishimura A, Okamoto M, Sugawara Y, Mizuno N, Yamauchi J, Itoh H: Ric-8A potentiates Gq-mediated signal transduction by acting downstream of G protein-coupled receptor in intact cells. Genes Cells 2006;11:487-498.
    • (2006) Genes Cells , vol.11 , pp. 487-498
    • Nishimura, A.1    Okamoto, M.2    Sugawara, Y.3    Mizuno, N.4    Yamauchi, J.5    Itoh, H.6
  • 58
    • 17644404436 scopus 로고    scopus 로고
    • Ric-8B, an olfactory putative GTP exchange factor, amplifies signal transduction through the olfactory-specific G-protein Gαolf
    • Von Dannecker LE, Mercadante AF, Malnic B: Ric-8B, an olfactory putative GTP exchange factor, amplifies signal transduction through the olfactory-specific G-protein Gαolf. J Neurosci 2005;25:3793-3800.
    • (2005) J Neurosci , vol.25 , pp. 3793-3800
    • Von Dannecker, L.E.1    Mercadante, A.F.2    Malnic, B.3
  • 60
    • 0034625373 scopus 로고    scopus 로고
    • Structure and function of sphingolipid- and cholesterol-rich membrane rafts
    • Brown DA, London E: Structure and function of sphingolipid- and cholesterol-rich membrane rafts. J Biol Chem 2000;275:17221-17224.
    • (2000) J Biol Chem , vol.275 , pp. 17221-17224
    • Brown, D.A.1    London, E.2
  • 61
    • 0035164003 scopus 로고    scopus 로고
    • Segregation of heterotrimeric G proteins in cell surface microdomains. Gq binds caveolin to concentrate in caveolae, whereas Gi and Gs target lipid rafts by default
    • Oh P, Schnitzer JE: Segregation of heterotrimeric G proteins in cell surface microdomains. Gq binds caveolin to concentrate in caveolae, whereas Gi and Gs target lipid rafts by default. Mol Biol Cell 2001;12:685-698.
    • (2001) Mol Biol Cell , vol.12 , pp. 685-698
    • Oh, P.1    Schnitzer, J.E.2
  • 62
    • 4644261120 scopus 로고    scopus 로고
    • Small interfering RNA-mediated down-regulation of caveolin-1 differentially modulates signaling pathways in endothelial cells
    • Gonzalez E, Nagiel A, Lin AJ, Golan DE, Michel T: Small interfering RNA-mediated down-regulation of caveolin-1 differentially modulates signaling pathways in endothelial cells. J Biol Chem 2004;279:40659-40669.
    • (2004) J Biol Chem , vol.279 , pp. 40659-40669
    • Gonzalez, E.1    Nagiel, A.2    Lin, A.J.3    Golan, D.E.4    Michel, T.5
  • 64
    • 34147166070 scopus 로고    scopus 로고
    • The lipid raft proteins flotillins/reggies interact with Gαq and are involved in Gq-mediated p38 mitogen-activated protein kinase activation through tyrosine kinase
    • Sugawara Y, Nishii H, Takahashi T, Yamauchi J, Mizuno N, Tago K, Itoh H: The lipid raft proteins flotillins/reggies interact with Gαq and are involved in Gq-mediated p38 mitogen-activated protein kinase activation through tyrosine kinase. Cell Signal 2007;19:1301-1308.
    • (2007) Cell Signal , vol.19 , pp. 1301-1308
    • Sugawara, Y.1    Nishii, H.2    Takahashi, T.3    Yamauchi, J.4    Mizuno, N.5    Tago, K.6    Itoh, H.7
  • 65
    • 0031054457 scopus 로고    scopus 로고
    • Reggie-1 and reggie-2, two cell surface proteins expressed by retinal ganglion cells during axon regeneration
    • Schulte T, Paschke KA, Laessing U, Lottspeich F, Stuermer CA: Reggie-1 and reggie-2, two cell surface proteins expressed by retinal ganglion cells during axon regeneration. Development 1997;124:577-587.
    • (1997) Development , vol.124 , pp. 577-587
    • Schulte, T.1    Paschke, K.A.2    Laessing, U.3    Lottspeich, F.4    Stuermer, C.A.5
  • 66
    • 0031010267 scopus 로고    scopus 로고
    • Flotillin and epidermal surface antigen define a new family of caveolae-associated integral membrane proteins
    • Bickel PE, Scherer PE, Schnitzer JE, Oh P, Lisanti MP, Lodish HF: Flotillin and epidermal surface antigen define a new family of caveolae-associated integral membrane proteins. J Biol Chem 1997;272:13793- 13802.
    • (1997) J Biol Chem , vol.272 , pp. 13793-13802
    • Bickel, P.E.1    Scherer, P.E.2    Schnitzer, J.E.3    Oh, P.4    Lisanti, M.P.5    Lodish, H.F.6
  • 67
    • 0001590871 scopus 로고    scopus 로고
    • The SPFH domain: Implicated in regulating targeted protein turnover in stomatins and other membrane-associated proteins
    • Tavernarakis N, Driscoll M, Kyrpides NC: The SPFH domain: implicated in regulating targeted protein turnover in stomatins and other membrane-associated proteins. Trends Biochem Sci 1999;24:425-427.
    • (1999) Trends Biochem Sci , vol.24 , pp. 425-427
    • Tavernarakis, N.1    Driscoll, M.2    Kyrpides, N.C.3
  • 68
    • 34548486955 scopus 로고    scopus 로고
    • The SPFH domain-containing proteins: More than lipid raft markers
    • Browman DT, Hoegg MB, Robbins SM: The SPFH domain-containing proteins: more than lipid raft markers. Trends Cell Biol 2007;17:394-402.
    • (2007) Trends Cell Biol , vol.17 , pp. 394-402
    • Browman, D.T.1    Hoegg, M.B.2    Robbins, S.M.3
  • 69
    • 0030784775 scopus 로고    scopus 로고
    • Activation of p38 mitogen-activated protein kinase by signaling through G protein-coupled receptors. Involvement of Gβγ and Gαq/11 subunits
    • Yamauchi J, Nagao M, Kaziro Y, Itoh H: Activation of p38 mitogen-activated protein kinase by signaling through G protein-coupled receptors. Involvement of Gβγ and Gαq/11 subunits. J Biol Chem 1997;272:27771-27777.
    • (1997) J Biol Chem , vol.272 , pp. 27771-27777
    • Yamauchi, J.1    Nagao, M.2    Kaziro, Y.3    Itoh, H.4
  • 70
    • 0032483381 scopus 로고    scopus 로고
    • Involvement of protein kinase C and Src family tyrosine kinase in Gαq/11-induced activation of c-Jun N-terminal kinase and p38 mitogen-activated protein kinase
    • Nagao M, Yamauchi J, Kaziro Y, Itoh H: Involvement of protein kinase C and Src family tyrosine kinase in Gαq/11-induced activation of c-Jun N-terminal kinase and p38 mitogen-activated protein kinase. J Biol Chem 1998;273:22892-22898.
    • (1998) J Biol Chem , vol.273 , pp. 22892-22898
    • Nagao, M.1    Yamauchi, J.2    Kaziro, Y.3    Itoh, H.4
  • 71
    • 0018654087 scopus 로고
    • Activation of adenylate cyclase by choleragen
    • Moss J, Vaughan M: Activation of adenylate cyclase by choleragen. Annu Rev Biochem 1979;48:581-600.
    • (1979) Annu Rev Biochem , vol.48 , pp. 581-600
    • Moss, J.1    Vaughan, M.2
  • 72
    • 0021321632 scopus 로고
    • Amino acid sequence of retinal transducin at the site ADP-ribosylated by cholera toxin
    • Van Dop C, Tsubokawa M, Bourne HR, Ramachandran J: Amino acid sequence of retinal transducin at the site ADP-ribosylated by cholera toxin. J Biol Chem 1984;259:696-698.
    • (1984) J Biol Chem , vol.259 , pp. 696-698
    • Van Dop, C.1    Tsubokawa, M.2    Bourne, H.R.3    Ramachandran, J.4
  • 73
    • 0020137319 scopus 로고
    • Direct modification of the membrane adenylate cyclase system by islet-activating protein due to ADP-ribosylation of a membrane protein
    • Katada T, Ui M: Direct modification of the membrane adenylate cyclase system by islet-activating protein due to ADP-ribosylation of a membrane protein. Proc Natl Acad Sci USA 1982;79:3129-3133.
    • (1982) Proc Natl Acad Sci USA , vol.79 , pp. 3129-3133
    • Katada, T.1    Ui, M.2
  • 74
    • 0020541131 scopus 로고
    • Specific uncoupling by islet-activating protein, pertussis toxin, of negative signal transduction via α-adrenergic, cholinergic, and opiate receptors in neuroblastoma x glioma hybrid cells
    • Kurose H, Katada T, Amano T, Ui M: Specific uncoupling by islet-activating protein, pertussis toxin, of negative signal transduction via α-adrenergic, cholinergic, and opiate receptors in neuroblastoma x glioma hybrid cells. J Biol Chem 1983;258:4870-4875.
    • (1983) J Biol Chem , vol.258 , pp. 4870-4875
    • Kurose, H.1    Katada, T.2    Amano, T.3    Ui, M.4
  • 75
    • 0031051444 scopus 로고    scopus 로고
    • Signalling functions and biochemical properties of pertussis toxin-resistant G-proteins
    • Fields TA, Casey PJ: Signalling functions and biochemical properties of pertussis toxin-resistant G-proteins. Biochem J 1997;321:561-571.
    • (1997) Biochem J , vol.321 , pp. 561-571
    • Fields, T.A.1    Casey, P.J.2
  • 76
    • 0026494325 scopus 로고
    • Pasteurella multocida toxin. The characterisation of the toxin and its significance in the diagnosis and prevention of progressive atrophic rhinitis in pigs
    • Foged NT: Pasteurella multocida toxin. The characterisation of the toxin and its significance in the diagnosis and prevention of progressive atrophic rhinitis in pigs. APMIS 1992;25(suppl):1-56.
    • (1992) APMIS , vol.25 , Issue.SUPPL. , pp. 1-56
    • Foged, N.T.1
  • 77
    • 6344235288 scopus 로고    scopus 로고
    • Regulation of osteoblast differentiation by Pasteurella multocida toxin (PMT): A role for Rho GTPase in bone formation
    • Harmey D, Stenbeck G, Nobes CD, Lax AJ, Grigoriadis AE: Regulation of osteoblast differentiation by Pasteurella multocida toxin (PMT): a role for Rho GTPase in bone formation. J Bone Miner Res 2004;19:661-670.
    • (2004) J Bone Miner Res , vol.19 , pp. 661-670
    • Harmey, D.1    Stenbeck, G.2    Nobes, C.D.3    Lax, A.J.4    Grigoriadis, A.E.5
  • 78
    • 2442699051 scopus 로고    scopus 로고
    • The Pasteurella multocida toxin interacts with signalling pathways to perturb cell growth and differentiation
    • Lax AJ, Pullinger GD, Baldwin MR, Harmey D, Grigoriadis AE, Lakey JH: The Pasteurella multocida toxin interacts with signalling pathways to perturb cell growth and differentiation. Int J Med Microbiol 2004;293:505-512.
    • (2004) Int J Med Microbiol , vol.293 , pp. 505-512
    • Lax, A.J.1    Pullinger, G.D.2    Baldwin, M.R.3    Harmey, D.4    Grigoriadis, A.E.5    Lakey, J.H.6
  • 80
    • 0031012747 scopus 로고    scopus 로고
    • Pasteurella multocida toxin activates the inositol triphosphate signaling pathway in Xenopus oocytes via Gqα-coupled phospholipase C-β1
    • Wilson BA, Zhu X, Ho M, Lu L: Pasteurella multocida toxin activates the inositol triphosphate signaling pathway in Xenopus oocytes via Gqα-coupled phospholipase C-β1. J Biol Chem 1997;272:1268-1275.
    • (1997) J Biol Chem , vol.272 , pp. 1268-1275
    • Wilson, B.A.1    Zhu, X.2    Ho, M.3    Lu, L.4
  • 81
    • 0026465679 scopus 로고
    • Pasteurella multocida toxin selectively facilitates phosphatidylinositol 4,5-bisphosphate hydrolysis by bombesin, vasopressin, and endothelin. Requirement for a functional G protein
    • Murphy AC, Rozengurt E: Pasteurella multocida toxin selectively facilitates phosphatidylinositol 4,5-bisphosphate hydrolysis by bombesin, vasopressin, and endothelin. Requirement for a functional G protein. J Biol Chem 1992;267:25296-25303.
    • (1992) J Biol Chem , vol.267 , pp. 25296-25303
    • Murphy, A.C.1    Rozengurt, E.2
  • 82
    • 21644478698 scopus 로고    scopus 로고
    • Pasteurella multocida toxin as a tool for studying Gq signal transduction
    • Wilson BA, Ho M: Pasteurella multocida toxin as a tool for studying Gq signal transduction. Rev Physiol Biochem Pharmacol 2004;152:93-109.
    • (2004) Rev Physiol Biochem Pharmacol , vol.152 , pp. 93-109
    • Wilson, B.A.1    Ho, M.2
  • 83
    • 0035830825 scopus 로고    scopus 로고
    • Pleiotropic effects of Pasteurella multocida toxin are mediated by Gq-dependent and -independent mechanisms. Involvement of Gq but not G11
    • Zywietz A, Gohla A, Schmelz M, Schultz G, Offermanns S: Pleiotropic effects of Pasteurella multocida toxin are mediated by Gq-dependent and -independent mechanisms. Involvement of Gq but not G11. J Biol Chem 2001;276:3840-3845.
    • (2001) J Biol Chem , vol.276 , pp. 3840-3845
    • Zywietz, A.1    Gohla, A.2    Schmelz, M.3    Schultz, G.4    Offermanns, S.5
  • 84
    • 4544253724 scopus 로고    scopus 로고
    • Action of Pasteurella multocida toxin depends on the helical domain of Gαq
    • Orth JH, Lang S, Aktories K: Action of Pasteurella multocida toxin depends on the helical domain of Gαq. J Biol Chem 2004;279:34150-34155.
    • (2004) J Biol Chem , vol.279 , pp. 34150-34155
    • Orth, J.H.1    Lang, S.2    Aktories, K.3
  • 85
    • 0032533479 scopus 로고    scopus 로고
    • Pasteurella multocida toxin increases endothelial permeability via Rho kinase and myosin light chain phosphatase
    • Essler M, Hermann K, Amano M, Kaibuchi K, Heesemann J, Weber PC, Aepfelbacher M: Pasteurella multocida toxin increases endothelial permeability via Rho kinase and myosin light chain phosphatase. J Immunol 1998;161:5640-5646.
    • (1998) J Immunol , vol.161 , pp. 5640-5646
    • Essler, M.1    Hermann, K.2    Amano, M.3    Kaibuchi, K.4    Heesemann, J.5    Weber, P.C.6    Aepfelbacher, M.7
  • 86
    • 0034695566 scopus 로고    scopus 로고
    • Pasteurella multocida toxin stimulates mitogen-activated protein kinase via Gq/11-dependent transactivation of the epidermal growth factor receptor
    • Seo B, Choy EW, Maudsley S, Miller WE, Wilson BA, Luttrell LM: Pasteurella multocida toxin stimulates mitogen-activated protein kinase via Gq/11-dependent transactivation of the epidermal growth factor receptor. J Biol Chem 2000;275:2239-2245.
    • (2000) J Biol Chem , vol.275 , pp. 2239-2245
    • Seo, B.1    Choy, E.W.2    Maudsley, S.3    Miller, W.E.4    Wilson, B.A.5    Luttrell, L.M.6
  • 87
    • 0030027455 scopus 로고    scopus 로고
    • Pasteurella multocida toxin, a potent intracellularly acting mitogen, induces p125FAK and paxillin tyrosine phosphorylation, actin stress fiber formation, and focal contact assembly in Swiss 3T3 cells
    • Lacerda HM, Lax AJ, Rozengurt E: Pasteurella multocida toxin, a potent intracellularly acting mitogen, induces p125FAK and paxillin tyrosine phosphorylation, actin stress fiber formation, and focal contact assembly in Swiss 3T3 cells. J Biol Chem 1996;271:439-445.
    • (1996) J Biol Chem , vol.271 , pp. 439-445
    • Lacerda, H.M.1    Lax, A.J.2    Rozengurt, E.3
  • 88
    • 0042206775 scopus 로고    scopus 로고
    • Receptor-dependent RhoA activation in G12/G13-deficient cells: Genetic evidence for an involvement of Gq/G11
    • Vogt S, Grosse R, Schultz G, Offermanns S: Receptor-dependent RhoA activation in G12/G13-deficient cells: genetic evidence for an involvement of Gq/G11. J Biol Chem 2003;278:28743-28749.
    • (2003) J Biol Chem , vol.278 , pp. 28743-28749
    • Vogt, S.1    Grosse, R.2    Schultz, G.3    Offermanns, S.4
  • 89
    • 0036261720 scopus 로고    scopus 로고
    • Leukemia-associated Rho guanine nucleotide exchange factor promotes Gαq-coupled activation of RhoA
    • Booden MA, Siderovski DP, Der CJ: Leukemia-associated Rho guanine nucleotide exchange factor promotes Gαq-coupled activation of RhoA. Mol Cell Biol 2002;22:4053-4061.
    • (2002) Mol Cell Biol , vol.22 , pp. 4053-4061
    • Booden, M.A.1    Siderovski, D.P.2    Der, C.J.3
  • 91
    • 27744535465 scopus 로고    scopus 로고
    • Pasteurella multocida toxin-induced activation of RhoA is mediated via two families of Gα proteins, Gαq and G α12/13
    • Orth JH, Lang S, Taniguchi M, Aktories K: Pasteurella multocida toxin-induced activation of RhoA is mediated via two families of Gα proteins, Gαq and G α12/13. J Biol Chem 2005;280:36701-36707.
    • (2005) J Biol Chem , vol.280 , pp. 36701-36707
    • Orth, J.H.1    Lang, S.2    Taniguchi, M.3    Aktories, K.4
  • 92
    • 0027176492 scopus 로고
    • Receptor-mediated binding of Pasteurella multocida dermonecrotic toxin to canine osteosarcoma and monkey kidney (vero) cells
    • Pettit RK, Ackermann MR, Rimler RB: Receptor-mediated binding of Pasteurella multocida dermonecrotic toxin to canine osteosarcoma and monkey kidney (vero) cells. Lab Invest 1993;69:94-100.
    • (1993) Lab Invest , vol.69 , pp. 94-100
    • Pettit, R.K.1    Ackermann, M.R.2    Rimler, R.B.3
  • 94
    • 43049145844 scopus 로고    scopus 로고
    • The C3 domain of Pasteurella multocida toxin is the minimal domain responsible for activation of Gq-dependent calcium and mitogenic signaling
    • Aminova LR, Luo S, Bannai Y, Ho M, Wilson BA: The C3 domain of Pasteurella multocida toxin is the minimal domain responsible for activation of Gq-dependent calcium and mitogenic signaling. Protein Sci 2008;17:945-949.
    • (2008) Protein Sci , vol.17 , pp. 945-949
    • Aminova, L.R.1    Luo, S.2    Bannai, Y.3    Ho, M.4    Wilson, B.A.5
  • 95
    • 0042357452 scopus 로고    scopus 로고
    • Pasteurella multocida toxin facilitates inositol phosphate formation by bombesin through tyrosine phosphorylation of Gαq
    • Baldwin MR, Pullinger GD, Lax AJ: Pasteurella multocida toxin facilitates inositol phosphate formation by bombesin through tyrosine phosphorylation of Gαq. J Biol Chem 2003;278:32719-32725.
    • (2003) J Biol Chem , vol.278 , pp. 32719-32725
    • Baldwin, M.R.1    Pullinger, G.D.2    Lax, A.J.3
  • 96
    • 34548379428 scopus 로고    scopus 로고
    • Action of Pasteurella multocida toxin on Gαq is persistent and independent of interaction with G-protein-coupled receptors
    • Orth JH, Lang S, Preuss I, Milligan G, Aktories K: Action of Pasteurella multocida toxin on Gαq is persistent and independent of interaction with G-protein-coupled receptors. Cell Signal 2007;19:2174-2182.
    • (2007) Cell Signal , vol.19 , pp. 2174-2182
    • Orth, J.H.1    Lang, S.2    Preuss, I.3    Milligan, G.4    Aktories, K.5
  • 101
    • 33646393236 scopus 로고    scopus 로고
    • Biological properties of a specific Gαq/11 inhibitor, YM-254890, on platelet functions and thrombus formation under high-shear stress
    • Uemura T, Kawasaki T, Taniguchi M, Moritani Y, Hayashi K, Saito T, Takasaki J, Uchida W, Miyata K: Biological properties of a specific Gαq/11 inhibitor, YM-254890, on platelet functions and thrombus formation under high-shear stress. Br J Pharmacol 2006;148:61-69.
    • (2006) Br J Pharmacol , vol.148 , pp. 61-69
    • Uemura, T.1    Kawasaki, T.2    Taniguchi, M.3    Moritani, Y.4    Hayashi, K.5    Saito, T.6    Takasaki, J.7    Uchida, W.8    Miyata, K.9
  • 104
    • 34548784426 scopus 로고    scopus 로고
    • Involvement of Gq/11 in both integrin signal-dependent and -independent pathways regulating endothelin-induced neural progenitor proliferation
    • Morishita R, Ueda H, Ito H, Takasaki J, Nagata K, Asano T: Involvement of Gq/11 in both integrin signal-dependent and -independent pathways regulating endothelin-induced neural progenitor proliferation. Neurosci Res 2007;59:205-214.
    • (2007) Neurosci Res , vol.59 , pp. 205-214
    • Morishita, R.1    Ueda, H.2    Ito, H.3    Takasaki, J.4    Nagata, K.5    Asano, T.6
  • 105
    • 34347360846 scopus 로고    scopus 로고
    • Gαq-mediated regulation of TASK3 two-pore domain potassium channels: The role of protein kinase C
    • Veale EL, Kennard LE, Sutton GL, Mac-Kenzie G, Sandu C, Mathie A: Gαq-mediated regulation of TASK3 two-pore domain potassium channels: the role of protein kinase C. Mol Pharmacol 2007;71:1666-1675.
    • (2007) Mol Pharmacol , vol.71 , pp. 1666-1675
    • Veale, E.L.1    Kennard, L.E.2    Sutton, G.L.3    Mac-Kenzie, G.4    Sandu, C.5    Mathie, A.6
  • 106
    • 0030756508 scopus 로고    scopus 로고
    • Defective platelet activation in Gαq-deficient mice
    • Offermanns S, Toombs CF, Hu YH, Simon MI: Defective platelet activation in Gαq-deficient mice. Nature 1997;389:183-186.
    • (1997) Nature , vol.389 , pp. 183-186
    • Offermanns, S.1    Toombs, C.F.2    Hu, Y.H.3    Simon, M.I.4
  • 108
    • 0032480009 scopus 로고    scopus 로고
    • Embryonic cardiomyocyte hypoplasia and craniofacial defects in Gαq/Gα11-mutant mice
    • Offermanns S, Zhao LP, Gohla A, Sarosi I, Simon MI, Wilkie TM: Embryonic cardiomyocyte hypoplasia and craniofacial defects in Gαq/Gα11-mutant mice. EMBO J 1998;17:4304-4312.
    • (1998) EMBO J , vol.17 , pp. 4304-4312
    • Offermanns, S.1    Zhao, L.P.2    Gohla, A.3    Sarosi, I.4    Simon, M.I.5    Wilkie, T.M.6
  • 110
    • 0346687569 scopus 로고    scopus 로고
    • Mouse models to study G-protein-mediated signaling
    • Wettschureck N, Moers A, Offermanns S: Mouse models to study G-protein-mediated signaling. Pharmacol Ther 2004;101:75-89.
    • (2004) Pharmacol Ther , vol.101 , pp. 75-89
    • Wettschureck, N.1    Moers, A.2    Offermanns, S.3
  • 111
  • 112
    • 14044266920 scopus 로고    scopus 로고
    • Loss of Gq/11 family G proteins in the nervous system causes pituitary somatotroph hypoplasia and dwarfism in mice
    • Wettschureck N, Moers A, Wallenwein B, Parlow AF, Maser-Gluth C, Offermanns S: Loss of Gq/11 family G proteins in the nervous system causes pituitary somatotroph hypoplasia and dwarfism in mice. Mol Cell Biol 2005;25:1942-1948.
    • (2005) Mol Cell Biol , vol.25 , pp. 1942-1948
    • Wettschureck, N.1    Moers, A.2    Wallenwein, B.3    Parlow, A.F.4    Maser-Gluth, C.5    Offermanns, S.6
  • 115
    • 33846861522 scopus 로고    scopus 로고
    • PACAP/PAC1 autocrine system promotes proliferation and astrogenesis in neural progenitor cells
    • Nishimoto M, Furuta A, Aoki S, Kudo Y, Miyakawa H, Wada K: PACAP/PAC1 autocrine system promotes proliferation and astrogenesis in neural progenitor cells. Glia 2007;55:317-327.
    • (2007) Glia , vol.55 , pp. 317-327
    • Nishimoto, M.1    Furuta, A.2    Aoki, S.3    Kudo, Y.4    Miyakawa, H.5    Wada, K.6
  • 116
    • 1942453322 scopus 로고    scopus 로고
    • Historical review: Endothelin
    • Masaki T: Historical review: endothelin. Trends Pharmacol Sci 2004;25:219-224.
    • (2004) Trends Pharmacol Sci , vol.25 , pp. 219-224
    • Masaki, T.1
  • 117
    • 0033518175 scopus 로고    scopus 로고
    • The temporal requirement for endothelin receptor-B signalling during neural crest development
    • Shin MK, Levorse JM, Ingram RS, Tilghman SM: The temporal requirement for endothelin receptor-B signalling during neural crest development. Nature 1999;402:496-501.
    • (1999) Nature , vol.402 , pp. 496-501
    • Shin, M.K.1    Levorse, J.M.2    Ingram, R.S.3    Tilghman, S.M.4
  • 119
    • 0037031651 scopus 로고    scopus 로고
    • New directions in neuronal migration
    • Hatten ME: New directions in neuronal migration. Science 2002;297:1660-1663.
    • (2002) Science , vol.297 , pp. 1660-1663
    • Hatten, M.E.1
  • 120
    • 0033821963 scopus 로고    scopus 로고
    • GABA receptor antagonists modulate postmitotic cell migration in slice cultures of embryonic rat cortex
    • Behar TN, Schaffner AE, Scott CA, Greene CL, Barker JL: GABA receptor antagonists modulate postmitotic cell migration in slice cultures of embryonic rat cortex. Cereb Cortex 2000;10:899-909.
    • (2000) Cereb Cortex , vol.10 , pp. 899-909
    • Behar, T.N.1    Schaffner, A.E.2    Scott, C.A.3    Greene, C.L.4    Barker, J.L.5
  • 123
    • 24644448307 scopus 로고    scopus 로고
    • KuroseH, Itoh H: G protein-coupled receptor signaling through Gq and JNK negatively regulates neural progenitor cell migration
    • Mizuno N, Kokubu,H, Sato M, Nishimura A, Yamauchi J, KuroseH, Itoh H: G protein-coupled receptor signaling through Gq and JNK negatively regulates neural progenitor cell migration. Proc Natl Acad Sci USA 2005;102:12365-12370.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 12365-12370
    • Mizuno, N.1    Kokubu, H.2    Sato, M.3    Nishimura, A.4    Yamauchi, J.5
  • 124
    • 0242442596 scopus 로고    scopus 로고
    • Multipolar migration: The third mode of radial neuronal migration in the developing cerebral cortex
    • Tabata H, Nakajima K: Multipolar migration: the third mode of radial neuronal migration in the developing cerebral cortex. J Neurosci 2003;23:9996-10001.
    • (2003) J Neurosci , vol.23 , pp. 9996-10001
    • Tabata, H.1    Nakajima, K.2
  • 125
    • 0036594138 scopus 로고    scopus 로고
    • Modes of neuronal migration in the developing cerebral cortex
    • Nadarajah B, Parnavelas JG: Modes of neuronal migration in the developing cerebral cortex. Nat Rev Neurosci 2002;3:423-432.
    • (2002) Nat Rev Neurosci , vol.3 , pp. 423-432
    • Nadarajah, B.1    Parnavelas, J.G.2
  • 127
    • 2342653563 scopus 로고    scopus 로고
    • Dynamic regulation of a GPCR-tetraspanin-G protein complex on intact cells: Central role of CD81 in facilitating GPR56-Gαq/11 association
    • Little KD, Hemler ME, Stipp CS: Dynamic regulation of a GPCR-tetraspanin-G protein complex on intact cells: central role of CD81 in facilitating GPR56-Gαq/11 association. Mol Biol Cell 2004;15:2375-2387.
    • (2004) Mol Biol Cell , vol.15 , pp. 2375-2387
    • Little, K.D.1    Hemler, M.E.2    Stipp, C.S.3
  • 128
    • 47249103800 scopus 로고    scopus 로고
    • Orphan G protein-coupled receptor GPR56 regulates neural progenitor cell migration via a Gα12/13 and Rho pathway
    • Iguchi T, Sakata K, Yoshizaki K, Tago K, Mizuno N, Itoh H: Orphan G protein-coupled receptor GPR56 regulates neural progenitor cell migration via a Gα12/13 and Rho pathway. J Biol Chem 2008;283:14469-14478.
    • (2008) J Biol Chem , vol.283 , pp. 14469-14478
    • Iguchi, T.1    Sakata, K.2    Yoshizaki, K.3    Tago, K.4    Mizuno, N.5    Itoh, H.6
  • 129
    • 53149130234 scopus 로고    scopus 로고
    • Activation of Gαi and subsequent uncoupling of receptor-Gαi signaling by Pasteurella multocida toxin
    • Orth JH, Fester I, Preuss I, Agnoletto L, Wilson BA, Aktories K: Activation of Gαi and subsequent uncoupling of receptor-Gαi signaling by Pasteurella multocida toxin. J Biol Chem 2008;283:23288-23294.
    • (2008) J Biol Chem , vol.283 , pp. 23288-23294
    • Orth, J.H.1    Fester, I.2    Preuss, I.3    Agnoletto, L.4    Wilson, B.A.5    Aktories, K.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.