메뉴 건너뛰기




Volumn 1815, Issue 2, 2011, Pages 170-188

The RasGrf family of mammalian guanine nucleotide exchange factors

Author keywords

Cell growth differentiation; Guanine nucleotide exchange factor; RasGEF; RasGrf1; RasGrf2; Signal transduction

Indexed keywords

CALCIUM; CANNABINOID RECEPTOR; CYCLIC AMP; G PROTEIN COUPLED RECEPTOR; GLUCOSE; GLUTAMATE RECEPTOR; GUANINE NUCLEOTIDE EXCHANGE FACTOR; PROTEIN RASGRF2; RAS PROTEIN; RHO GUANINE NUCLEOTIDE BINDING PROTEIN; UNCLASSIFIED DRUG;

EID: 78651379505     PISSN: 0304419X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbcan.2010.11.001     Document Type: Review
Times cited : (83)

References (161)
  • 2
    • 0023155907 scopus 로고
    • CDC25: a component of the RAS-adenylate cyclase pathway in Saccharomyces cerevisiae
    • Robinson L.C., Gibbs J.B., Marshall M.S., Sigal I.S., Tatchell K. CDC25: a component of the RAS-adenylate cyclase pathway in Saccharomyces cerevisiae. Science 1987, 235:1218-1221.
    • (1987) Science , vol.235 , pp. 1218-1221
    • Robinson, L.C.1    Gibbs, J.B.2    Marshall, M.S.3    Sigal, I.S.4    Tatchell, K.5
  • 3
    • 0025277948 scopus 로고
    • A cytosolic protein catalyzes the release of GDP from p21ras
    • Wolfman A., Macara I.G. A cytosolic protein catalyzes the release of GDP from p21ras. Science 1990, 248:67-69.
    • (1990) Science , vol.248 , pp. 67-69
    • Wolfman, A.1    Macara, I.G.2
  • 4
    • 0025186360 scopus 로고
    • Purification of a factor capable of stimulating the guanine nucleotide exchange reaction of ras proteins and its effect on ras-related small molecular mass G proteins
    • Huang Y.K., Kung H.F., Kamata T. Purification of a factor capable of stimulating the guanine nucleotide exchange reaction of ras proteins and its effect on ras-related small molecular mass G proteins. Proc. Natl Acad. Sci. USA 1990, 87:8008-8012.
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 8008-8012
    • Huang, Y.K.1    Kung, H.F.2    Kamata, T.3
  • 5
    • 0026523616 scopus 로고
    • Cloning by functional complementation of a mouse cDNA encoding a homologue of CDC25, a Saccharomyces cerevisiae RAS activator
    • Martegani E., Vanoni M., Zippel R., Coccetti P., Brambilla R., Ferrari C., Sturani E., Alberghina L. Cloning by functional complementation of a mouse cDNA encoding a homologue of CDC25, a Saccharomyces cerevisiae RAS activator. EMBO J. 1992, 11:2151-2157.
    • (1992) EMBO J. , vol.11 , pp. 2151-2157
    • Martegani, E.1    Vanoni, M.2    Zippel, R.3    Coccetti, P.4    Brambilla, R.5    Ferrari, C.6    Sturani, E.7    Alberghina, L.8
  • 7
    • 0027365376 scopus 로고
    • A murine CDC25/ras-GRF-related protein implicated in Ras regulation
    • Chen L., Zhang L.J., Greer P., Tung P.S., Moran M.F. A murine CDC25/ras-GRF-related protein implicated in Ras regulation. Dev. Genet. 1993, 14:339-346.
    • (1993) Dev. Genet. , vol.14 , pp. 339-346
    • Chen, L.1    Zhang, L.J.2    Greer, P.3    Tung, P.S.4    Moran, M.F.5
  • 8
    • 0031026133 scopus 로고    scopus 로고
    • Cloning and characterization of Ras-GRF2, a novel guanine nucleotide exchange factor for Ras
    • Fam N.P., Fan W.-T., Wang Z., Zhang L.-J., Chen H., Moran M.F. Cloning and characterization of Ras-GRF2, a novel guanine nucleotide exchange factor for Ras. Mol. Cell. Biol. 1997, 17:1396-1406.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 1396-1406
    • Fam, N.P.1    Fan, W.-T.2    Wang, Z.3    Zhang, L.-J.4    Chen, H.5    Moran, M.F.6
  • 9
    • 0026768072 scopus 로고
    • Isolation of multiple mouse cDNAs with coding homology to Sacharomyces cerevisiae CDC25: identification of a region related to Bcr, Vav, Dbl and CDC24
    • Cen H., Papageorge A.G., Zippel R., Lowy D.R., Zhang K. Isolation of multiple mouse cDNAs with coding homology to Sacharomyces cerevisiae CDC25: identification of a region related to Bcr, Vav, Dbl and CDC24. EMBO J. 1992, 11:4007-4015.
    • (1992) EMBO J. , vol.11 , pp. 4007-4015
    • Cen, H.1    Papageorge, A.G.2    Zippel, R.3    Lowy, D.R.4    Zhang, K.5
  • 10
    • 0031582212 scopus 로고    scopus 로고
    • Activation of the exchange factor Ras-GRF by calcium requires an intact Dbl homolgy domain
    • Freshney N.W., Goonesekera S.D., Feig L.A. Activation of the exchange factor Ras-GRF by calcium requires an intact Dbl homolgy domain. FEBS Lett. 1997, 407:111-115.
    • (1997) FEBS Lett. , vol.407 , pp. 111-115
    • Freshney, N.W.1    Goonesekera, S.D.2    Feig, L.A.3
  • 11
    • 0027491578 scopus 로고
    • Comparison of kinetic properties between two mammalian ras p21 GDP/GTP exchange proteins, ras guanine nucleotide-releasing factor and smg GDP dissociation stimulation
    • Orita S., Kaibuchi K., Kuroda S., Shimizu K., Nakanishi H., Takai Y. Comparison of kinetic properties between two mammalian ras p21 GDP/GTP exchange proteins, ras guanine nucleotide-releasing factor and smg GDP dissociation stimulation. J. Biol. Chem. 1993, 268:25542-25546.
    • (1993) J. Biol. Chem. , vol.268 , pp. 25542-25546
    • Orita, S.1    Kaibuchi, K.2    Kuroda, S.3    Shimizu, K.4    Nakanishi, H.5    Takai, Y.6
  • 12
    • 13144250140 scopus 로고    scopus 로고
    • The exchange factor Ras-GRF2 activates Ras-dependent and Rac-dependent mitogen-activated protein kinase pathways
    • Fan W., Koch C.A., de Hoog C.L., Fam N.P., Moran M.F. The exchange factor Ras-GRF2 activates Ras-dependent and Rac-dependent mitogen-activated protein kinase pathways. Curr. Biol. 1998, 8:935-938.
    • (1998) Curr. Biol. , vol.8 , pp. 935-938
    • Fan, W.1    Koch, C.A.2    de Hoog, C.L.3    Fam, N.P.4    Moran, M.F.5
  • 13
    • 0032722971 scopus 로고    scopus 로고
    • CDC25(Mm)/Ras-GRF1 regulates both Ras and Rac signaling pathways
    • Innocenti M., Zippel R., Brambilla R., Sturani E. CDC25(Mm)/Ras-GRF1 regulates both Ras and Rac signaling pathways. FEBS Lett. 1999, 460:357-362.
    • (1999) FEBS Lett. , vol.460 , pp. 357-362
    • Innocenti, M.1    Zippel, R.2    Brambilla, R.3    Sturani, E.4
  • 14
    • 0033608990 scopus 로고    scopus 로고
    • G protein beta gamma subunit-dependent Rac-guanine nucleotide exchange activity of Ras-GRF1/CDC25(Mm)
    • Kiyono M., Satoh T., Kaziro Y. G protein beta gamma subunit-dependent Rac-guanine nucleotide exchange activity of Ras-GRF1/CDC25(Mm). Proc. Natl Acad. Sci. USA 1999, 96:4826-4831.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 4826-4831
    • Kiyono, M.1    Satoh, T.2    Kaziro, Y.3
  • 22
    • 32544453670 scopus 로고    scopus 로고
    • Distinct roles for Ras-guanine nucleotide-releasing factor 1 (Ras-GRF1) and Ras-GRF2 in the induction of long-term potentiation and long-term depression
    • Li S., Tian X., Hartley D.M., Feig L.A. Distinct roles for Ras-guanine nucleotide-releasing factor 1 (Ras-GRF1) and Ras-GRF2 in the induction of long-term potentiation and long-term depression. J. Neurosci. 2006, 26:1721-1729.
    • (2006) J. Neurosci. , vol.26 , pp. 1721-1729
    • Li, S.1    Tian, X.2    Hartley, D.M.3    Feig, L.A.4
  • 23
    • 36849018399 scopus 로고    scopus 로고
    • RasGRF2, a guanosine nucleotide exchange factor for Ras GTPases, participates in T-cell signaling responses
    • Ruiz S., Santos E., Bustelo X.R. RasGRF2, a guanosine nucleotide exchange factor for Ras GTPases, participates in T-cell signaling responses. Mol. Cell. Biol. 2007, 27:8127-8142.
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 8127-8142
    • Ruiz, S.1    Santos, E.2    Bustelo, X.R.3
  • 24
    • 77949535231 scopus 로고    scopus 로고
    • The use of knockout mice reveals a synergistic role of the Vav1 and Rasgrf2 gene deficiencies in lymphomagenesis and metastasis
    • Ruiz S., Santos E., Bustelo X.R. The use of knockout mice reveals a synergistic role of the Vav1 and Rasgrf2 gene deficiencies in lymphomagenesis and metastasis. PLoS ONE 2009, 4:e8229.
    • (2009) PLoS ONE , vol.4
    • Ruiz, S.1    Santos, E.2    Bustelo, X.R.3
  • 26
    • 16244392404 scopus 로고    scopus 로고
    • P75-Ras-GRF1 is a c-Jun/AP-1 target protein: it's up regulation results in increased Ras activity and is necessary for c-Jun-induced nonadherent growth of Rat1a cells
    • Leaner V.D., Donninger H., Ellis C.A., Clark G.J., Birrer M.J. p75-Ras-GRF1 is a c-Jun/AP-1 target protein: it's up regulation results in increased Ras activity and is necessary for c-Jun-induced nonadherent growth of Rat1a cells. Mol. Cell. Biol. 2005, 25:3324-3337.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 3324-3337
    • Leaner, V.D.1    Donninger, H.2    Ellis, C.A.3    Clark, G.J.4    Birrer, M.J.5
  • 27
    • 0033609571 scopus 로고    scopus 로고
    • GRFbeta, a novel regulator of calcium signaling, is expressed in pancreatic beta cells and brain
    • Arava Y., Seger R., Walker M.D. GRFbeta, a novel regulator of calcium signaling, is expressed in pancreatic beta cells and brain. J. Biol. Chem. 1999, 274:24449-24452.
    • (1999) J. Biol. Chem. , vol.274 , pp. 24449-24452
    • Arava, Y.1    Seger, R.2    Walker, M.D.3
  • 29
    • 0026659515 scopus 로고
    • Molecular cloning of cDNAs encoding a guanine-nucleotide-releasing factor for Ras p21
    • Shou C., Farnsworth C.L., Neel B.G., Feig L.A. Molecular cloning of cDNAs encoding a guanine-nucleotide-releasing factor for Ras p21. Nature 1992, 358:351-354.
    • (1992) Nature , vol.358 , pp. 351-354
    • Shou, C.1    Farnsworth, C.L.2    Neel, B.G.3    Feig, L.A.4
  • 30
    • 0031017165 scopus 로고    scopus 로고
    • Mapping of the Ras-GRF2 gene (GRF2) to mouse chromosome 13C3-D1 and human chromosome 5q13, near the Ras-GAP gene
    • Fam N.P., Zhang L.-J., Rommens J.M., Beatty B.G., Moran M.F. Mapping of the Ras-GRF2 gene (GRF2) to mouse chromosome 13C3-D1 and human chromosome 5q13, near the Ras-GAP gene. Genomics 1997, 39:118-120.
    • (1997) Genomics , vol.39 , pp. 118-120
    • Fam, N.P.1    Zhang, L.-J.2    Rommens, J.M.3    Beatty, B.G.4    Moran, M.F.5
  • 31
    • 3042584653 scopus 로고    scopus 로고
    • Essential role for de novo DNA methyltransferase Dnmt3a in paternal and maternal imprinting
    • Kaneda M., Okano M., Hata K., Sado T., Tsujimoto N., Li E., Sasaki H. Essential role for de novo DNA methyltransferase Dnmt3a in paternal and maternal imprinting. Nature 2004, 429:900-903.
    • (2004) Nature , vol.429 , pp. 900-903
    • Kaneda, M.1    Okano, M.2    Hata, K.3    Sado, T.4    Tsujimoto, N.5    Li, E.6    Sasaki, H.7
  • 33
    • 7944221225 scopus 로고    scopus 로고
    • Timing of establishment of paternal methylation imprints in the mouse
    • Li J.Y., Lees-Murdock D.J., Xu G.L., Walsh C.P. Timing of establishment of paternal methylation imprints in the mouse. Genomics 2004, 84:952-960.
    • (2004) Genomics , vol.84 , pp. 952-960
    • Li, J.Y.1    Lees-Murdock, D.J.2    Xu, G.L.3    Walsh, C.P.4
  • 35
    • 33845456113 scopus 로고    scopus 로고
    • Timing and sequence requirements defined for embryonic maintenance of imprinted DNA methylation at Rasgrf1
    • Holmes R., Chang Y., Soloway P.D. Timing and sequence requirements defined for embryonic maintenance of imprinted DNA methylation at Rasgrf1. Mol. Cell. Biol. 2006, 26:9564-9570.
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 9564-9570
    • Holmes, R.1    Chang, Y.2    Soloway, P.D.3
  • 39
    • 61549097838 scopus 로고    scopus 로고
    • Transcriptomic and proteomic analyses of mouse cerebellum reveals alterations in RasGRF1 expression following in vivo chronic treatment with delta 9-tetrahydrocannabinol
    • Colombo G., Rusconi F., Rubino T., Cattaneo A., Martegani E., Parolaro D., Bachi A., Zippel R. Transcriptomic and proteomic analyses of mouse cerebellum reveals alterations in RasGRF1 expression following in vivo chronic treatment with delta 9-tetrahydrocannabinol. J. Mol. Neurosci. 2009, 37:111-122.
    • (2009) J. Mol. Neurosci. , vol.37 , pp. 111-122
    • Colombo, G.1    Rusconi, F.2    Rubino, T.3    Cattaneo, A.4    Martegani, E.5    Parolaro, D.6    Bachi, A.7    Zippel, R.8
  • 40
    • 69749126952 scopus 로고    scopus 로고
    • Amphetamine alters Ras-guanine nucleotide-releasing factor expression in the rat striatum in vivo
    • Parelkar N.K., Jiang Q., Chu X.P., Guo M.L., Mao L.M., Wang J.Q. Amphetamine alters Ras-guanine nucleotide-releasing factor expression in the rat striatum in vivo. Eur. J. Pharmacol. 2009, 619:50-56.
    • (2009) Eur. J. Pharmacol. , vol.619 , pp. 50-56
    • Parelkar, N.K.1    Jiang, Q.2    Chu, X.P.3    Guo, M.L.4    Mao, L.M.5    Wang, J.Q.6
  • 41
    • 35449002763 scopus 로고    scopus 로고
    • Cocaine increases Ras-guanine nucleotide-releasing factor 1 protein expression in the rat striatum in vivo
    • Zhang G.C., Hoffmann J., Parelkar N.K., Liu X.Y., Mao L.M., Fibuch E.E., Wang J.Q. Cocaine increases Ras-guanine nucleotide-releasing factor 1 protein expression in the rat striatum in vivo. Neurosci. Lett. 2007, 427:117-121.
    • (2007) Neurosci. Lett. , vol.427 , pp. 117-121
    • Zhang, G.C.1    Hoffmann, J.2    Parelkar, N.K.3    Liu, X.Y.4    Mao, L.M.5    Fibuch, E.E.6    Wang, J.Q.7
  • 42
    • 0036759157 scopus 로고    scopus 로고
    • Lack of neurodegeneration in transgenic mice overexpressing mutant amyloid precursor protein is associated with increased levels of transthyretin and the activation of cell survival pathways
    • Stein T.D., Johnson J.A. Lack of neurodegeneration in transgenic mice overexpressing mutant amyloid precursor protein is associated with increased levels of transthyretin and the activation of cell survival pathways. J. Neurosci. 2002, 22:7380-7388.
    • (2002) J. Neurosci. , vol.22 , pp. 7380-7388
    • Stein, T.D.1    Johnson, J.A.2
  • 43
    • 33744915584 scopus 로고    scopus 로고
    • Sustained trophism of the mammary gland is sufficient to accelerate and synchronize development of ErbB2/Neu-induced tumors
    • Landis M.D., Seachrist D.D., Abdul-Karim F.W., Keri R.A. Sustained trophism of the mammary gland is sufficient to accelerate and synchronize development of ErbB2/Neu-induced tumors. Oncogene 2006, 25:3325-3334.
    • (2006) Oncogene , vol.25 , pp. 3325-3334
    • Landis, M.D.1    Seachrist, D.D.2    Abdul-Karim, F.W.3    Keri, R.A.4
  • 44
    • 58149462796 scopus 로고    scopus 로고
    • Translational responses of NR2B overexpression in the cerebral cortex of transgenic mice: a liquid chromatography-based proteomic approach
    • Gu F., Shi J., Wen Y., Fan H., Hu J., Hu Y., Zhao Z. Translational responses of NR2B overexpression in the cerebral cortex of transgenic mice: a liquid chromatography-based proteomic approach. Brain Res. 2009, 1250:1-13.
    • (2009) Brain Res. , vol.1250 , pp. 1-13
    • Gu, F.1    Shi, J.2    Wen, Y.3    Fan, H.4    Hu, J.5    Hu, Y.6    Zhao, Z.7
  • 47
    • 37549066863 scopus 로고    scopus 로고
    • Discovery of epigenetically silenced genes by methylated DNA immunoprecipitation in colon cancer cells
    • Jacinto F.V., Ballestar E., Ropero S., Esteller M. Discovery of epigenetically silenced genes by methylated DNA immunoprecipitation in colon cancer cells. Cancer Res. 2007, 67:11481-11486.
    • (2007) Cancer Res. , vol.67 , pp. 11481-11486
    • Jacinto, F.V.1    Ballestar, E.2    Ropero, S.3    Esteller, M.4
  • 48
    • 2342561884 scopus 로고    scopus 로고
    • Developmentally regulated role for Ras-GRFs in coupling NMDA glutamate receptors to Ras, Erk and CREB
    • Tian X., Gotoh T., Tsuji K., Lo E.H., Huang S., Feig L.A. Developmentally regulated role for Ras-GRFs in coupling NMDA glutamate receptors to Ras, Erk and CREB. EMBO J. 2004, 23:1567-1575.
    • (2004) EMBO J. , vol.23 , pp. 1567-1575
    • Tian, X.1    Gotoh, T.2    Tsuji, K.3    Lo, E.H.4    Huang, S.5    Feig, L.A.6
  • 49
    • 0347087356 scopus 로고    scopus 로고
    • Identification of differentially regulated transcripts in mouse striatum following methamphetamine treatment-an oligonucleotide microarray approach
    • Thomas D.M., Francescutti-Verbeem D.M., Liu X., Kuhn D.M. Identification of differentially regulated transcripts in mouse striatum following methamphetamine treatment-an oligonucleotide microarray approach. J. Neurochem. 2004, 88:380-393.
    • (2004) J. Neurochem. , vol.88 , pp. 380-393
    • Thomas, D.M.1    Francescutti-Verbeem, D.M.2    Liu, X.3    Kuhn, D.M.4
  • 50
    • 0028304947 scopus 로고
    • Expression of two different products of CDC25 Mm, a mammalian Ras activator, during development of mouse brain
    • Ferrari C., Zippel R., Martegani E., Gnesutta N., Carrera V., Sturani E. Expression of two different products of CDC25 Mm, a mammalian Ras activator, during development of mouse brain. Exp. Cell Res. 1994, 210:353-357.
    • (1994) Exp. Cell Res. , vol.210 , pp. 353-357
    • Ferrari, C.1    Zippel, R.2    Martegani, E.3    Gnesutta, N.4    Carrera, V.5    Sturani, E.6
  • 52
    • 0026741882 scopus 로고
    • Anti-Cdc25 antibodies inhibit guanyl nucleotide-dependent adenylyl cyclase of Saccharomyces cerevisiae and cross-react with a 150-kilodalton mammalian protein
    • Gross E., Marbach I., Engelberg D., Segal M., Simchen G., Levitzki A. Anti-Cdc25 antibodies inhibit guanyl nucleotide-dependent adenylyl cyclase of Saccharomyces cerevisiae and cross-react with a 150-kilodalton mammalian protein. Mol. Cell. Biol. 1992, 12:2653-2661.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 2653-2661
    • Gross, E.1    Marbach, I.2    Engelberg, D.3    Segal, M.4    Simchen, G.5    Levitzki, A.6
  • 53
    • 0027220836 scopus 로고
    • Localization of the cellular expression pattern of cdc25NEF and Ras in the juvenile rat brain
    • Wei W., Schreiber S.S., Baudry M., Tocco G., Broek D. Localization of the cellular expression pattern of cdc25NEF and Ras in the juvenile rat brain. Brain Res. Mol. Brain Res. 1993, 19:339-344.
    • (1993) Brain Res. Mol. Brain Res. , vol.19 , pp. 339-344
    • Wei, W.1    Schreiber, S.S.2    Baudry, M.3    Tocco, G.4    Broek, D.5
  • 55
    • 0030765356 scopus 로고    scopus 로고
    • A 54-kDa protein related to ras-guanine nucleotide release factor expressed in the rat exocine pancreas
    • Tung P.S., Fam N.P., Chen L., Moran M.F. A 54-kDa protein related to ras-guanine nucleotide release factor expressed in the rat exocine pancreas. Cell Tissue Res. 1997, 289:505-515.
    • (1997) Cell Tissue Res. , vol.289 , pp. 505-515
    • Tung, P.S.1    Fam, N.P.2    Chen, L.3    Moran, M.F.4
  • 56
    • 34447549291 scopus 로고    scopus 로고
    • Filamin A-mediated down-regulation of the exchange factor Ras-GRF1 correlates with decreased matrix metalloproteinase-9 expression in human melanoma cells
    • Zhu T.N., He H.J., Kole S., D'Souza T., Agarwal R., Morin P.J., Bernier M. Filamin A-mediated down-regulation of the exchange factor Ras-GRF1 correlates with decreased matrix metalloproteinase-9 expression in human melanoma cells. J. Biol. Chem. 2007, 282:14816-14826.
    • (2007) J. Biol. Chem. , vol.282 , pp. 14816-14826
    • Zhu, T.N.1    He, H.J.2    Kole, S.3    D'Souza, T.4    Agarwal, R.5    Morin, P.J.6    Bernier, M.7
  • 57
    • 0033002199 scopus 로고    scopus 로고
    • Ras-specific exchange factor GRF: oligomerization through its dbl homology domain and calcium-dependent activation of Raf
    • Anborgh P.H., Qian X., Papageorge A.G., Vass W.C., DeClue J.E., Lowy D.R. Ras-specific exchange factor GRF: oligomerization through its dbl homology domain and calcium-dependent activation of Raf. Mol. Cell. Biol. 1999, 19:4611-4622.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 4611-4622
    • Anborgh, P.H.1    Qian, X.2    Papageorge, A.G.3    Vass, W.C.4    DeClue, J.E.5    Lowy, D.R.6
  • 58
    • 0030996229 scopus 로고    scopus 로고
    • The N-terminal moiety of CDC25(Mm), a GDP/GTP exchange factor of Ras proteins, controls the activity of the catalytic domain. Modulation by calmodulin and calpain
    • Baouz S., Jacquet E., Bernardi A., Parmeggiani A. The N-terminal moiety of CDC25(Mm), a GDP/GTP exchange factor of Ras proteins, controls the activity of the catalytic domain. Modulation by calmodulin and calpain. J. Biol. Chem. 1997, 272:6671-6676.
    • (1997) J. Biol. Chem. , vol.272 , pp. 6671-6676
    • Baouz, S.1    Jacquet, E.2    Bernardi, A.3    Parmeggiani, A.4
  • 60
    • 0347034082 scopus 로고    scopus 로고
    • Cloning and characterization of mouse UBPy, a deubiquitinating enzyme that interacts with the ras guanine nucleotide exchange factor CDC25(Mm)/Ras-GRF1
    • Gnesutta N., Ceriani M., Innocenti M., Mauri I., Zippel R., Sturani E., Borgonovo B., Berruti G., Martegani E. Cloning and characterization of mouse UBPy, a deubiquitinating enzyme that interacts with the ras guanine nucleotide exchange factor CDC25(Mm)/Ras-GRF1. J. Biol. Chem. 2001, 276:39448-39454.
    • (2001) J. Biol. Chem. , vol.276 , pp. 39448-39454
    • Gnesutta, N.1    Ceriani, M.2    Innocenti, M.3    Mauri, I.4    Zippel, R.5    Sturani, E.6    Borgonovo, B.7    Berruti, G.8    Martegani, E.9
  • 61
    • 34250184630 scopus 로고    scopus 로고
    • Neuronal nuclear organization is controlled by cyclin-dependent kinase 5 phosphorylation of Ras guanine nucleotide releasing factor-1
    • Kesavapany S., Pareek T.K., Zheng Y.L., Amin N., Gutkind J.S., Ma W., Kulkarni A.B., Grant P., Pant H.C. Neuronal nuclear organization is controlled by cyclin-dependent kinase 5 phosphorylation of Ras guanine nucleotide releasing factor-1. Neurosignals 2006, 15:157-173.
    • (2006) Neurosignals , vol.15 , pp. 157-173
    • Kesavapany, S.1    Pareek, T.K.2    Zheng, Y.L.3    Amin, N.4    Gutkind, J.S.5    Ma, W.6    Kulkarni, A.B.7    Grant, P.8    Pant, H.C.9
  • 62
    • 2342494271 scopus 로고    scopus 로고
    • P35/cyclin-dependent kinase 5 phosphorylation of ras guanine nucleotide releasing factor 2 (RasGRF2) mediates Rac-dependent extracellular signal-regulated kinase 1/2 activity, altering RasGRF2 and microtubule-associated protein 1b distribution in neurons
    • Kesavapany S., Amin N., Zheng Y.L., Nijhara R., Jaffe H., Sihag R., Gutkind J.S., Takahashi S., Kulkarni A., Grant P., Pant H.C. p35/cyclin-dependent kinase 5 phosphorylation of ras guanine nucleotide releasing factor 2 (RasGRF2) mediates Rac-dependent extracellular signal-regulated kinase 1/2 activity, altering RasGRF2 and microtubule-associated protein 1b distribution in neurons. J. Neurosci. 2004, 24:4421-4431.
    • (2004) J. Neurosci. , vol.24 , pp. 4421-4431
    • Kesavapany, S.1    Amin, N.2    Zheng, Y.L.3    Nijhara, R.4    Jaffe, H.5    Sihag, R.6    Gutkind, J.S.7    Takahashi, S.8    Kulkarni, A.9    Grant, P.10    Pant, H.C.11
  • 63
    • 0031302711 scopus 로고    scopus 로고
    • Functional diversity of PH domains: an exhaustive modelling study
    • Blomberg N., Nilges M. Functional diversity of PH domains: an exhaustive modelling study. Fold. Des. 1997, 2:343-355.
    • (1997) Fold. Des. , vol.2 , pp. 343-355
    • Blomberg, N.1    Nilges, M.2
  • 64
    • 0028021882 scopus 로고
    • Pleckstrin homology domains bind to phosphatidylinositol-4, 5-bisphosphate
    • Harlan J.E., Hajduk P.J., Yoon H.S., Fesik S.W. Pleckstrin homology domains bind to phosphatidylinositol-4, 5-bisphosphate. Nature 1994, 371:168-170.
    • (1994) Nature , vol.371 , pp. 168-170
    • Harlan, J.E.1    Hajduk, P.J.2    Yoon, H.S.3    Fesik, S.W.4
  • 65
    • 0034663568 scopus 로고    scopus 로고
    • Signal-dependent membrane targeting by pleckstrin homology (PH) domains
    • Lemmon M.A., Ferguson K.M. Signal-dependent membrane targeting by pleckstrin homology (PH) domains. Biochem. J. 2000, 350(Pt 1):1-18.
    • (2000) Biochem. J. , vol.350 , Issue.PART 1 , pp. 1-18
    • Lemmon, M.A.1    Ferguson, K.M.2
  • 66
    • 0035850897 scopus 로고    scopus 로고
    • Specificity in pleckstrin homology (PH) domain membrane targeting: a role for a phosphoinositide-protein co-operative mechanism
    • Maffucci T., Falasca M. Specificity in pleckstrin homology (PH) domain membrane targeting: a role for a phosphoinositide-protein co-operative mechanism. FEBS Lett. 2001, 506:173-179.
    • (2001) FEBS Lett. , vol.506 , pp. 173-179
    • Maffucci, T.1    Falasca, M.2
  • 67
    • 0027367141 scopus 로고
    • Regulated and constitutive activity by CDC25Mm (GRF), a Ras-specific exchange factor
    • Cen H., Papageorge A.G., Vass W.C., Zhang K.E., Lowy D.R. Regulated and constitutive activity by CDC25Mm (GRF), a Ras-specific exchange factor. Mol. Cell. Biol. 1993, 13:7718-7724.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 7718-7724
    • Cen, H.1    Papageorge, A.G.2    Vass, W.C.3    Zhang, K.E.4    Lowy, D.R.5
  • 68
    • 79952443648 scopus 로고
    • Gβγ interactions with PH domains and Ras-MAPK signaling pathways
    • Inglese J., Koch J., Touhara K., Lefkowitz R.J. Gβγ interactions with PH domains and Ras-MAPK signaling pathways. FEBS Lett. 1995, 460:357-362.
    • (1995) FEBS Lett. , vol.460 , pp. 357-362
    • Inglese, J.1    Koch, J.2    Touhara, K.3    Lefkowitz, R.J.4
  • 69
    • 0032908296 scopus 로고    scopus 로고
    • Interaction between Pleckstrin homology domains and G protein betagamma-subunits: analyses of kinetic parameters by a biosensor-based method
    • Sawai T., Hirakawa T., Yamada K., Nishizawa Y. Interaction between Pleckstrin homology domains and G protein betagamma-subunits: analyses of kinetic parameters by a biosensor-based method. Biol. Pharm. Bull. 1999, 22:229-233.
    • (1999) Biol. Pharm. Bull. , vol.22 , pp. 229-233
    • Sawai, T.1    Hirakawa, T.2    Yamada, K.3    Nishizawa, Y.4
  • 70
    • 0028246440 scopus 로고
    • Binding of G protein beta gamma-subunits to pleckstrin homology domains
    • Touhara K., Inglese J., Pitcher J.A., Shaw G., Lefkowitz R.J. Binding of G protein beta gamma-subunits to pleckstrin homology domains. J. Biol. Chem. 1994, 269:10217-10220.
    • (1994) J. Biol. Chem. , vol.269 , pp. 10217-10220
    • Touhara, K.1    Inglese, J.2    Pitcher, J.A.3    Shaw, G.4    Lefkowitz, R.J.5
  • 72
    • 0029742101 scopus 로고    scopus 로고
    • The N-terminal pleckstrin, coiled-coil, and IQ domains of the exchange factor Ras-GRF act cooperatively to facilitate activation by calcium
    • Buchsbaum R., Telliez J.-B., Goonesekera S., Feig L.A. The N-terminal pleckstrin, coiled-coil, and IQ domains of the exchange factor Ras-GRF act cooperatively to facilitate activation by calcium. Mol. Cell. Biol. 1996, 16:4888-4896.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 4888-4896
    • Buchsbaum, R.1    Telliez, J.-B.2    Goonesekera, S.3    Feig, L.A.4
  • 73
    • 0036265520 scopus 로고    scopus 로고
    • Interaction of Rac exchange factors Tiam1 and Ras-GRF1 with a scaffold for the p38 mitogen-activated protein kinase cascade
    • Buchsbaum R.J., Connolly B.A., Feig L.A. Interaction of Rac exchange factors Tiam1 and Ras-GRF1 with a scaffold for the p38 mitogen-activated protein kinase cascade. Mol. Cell. Biol. 2002, 22:4073-4085.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 4073-4085
    • Buchsbaum, R.J.1    Connolly, B.A.2    Feig, L.A.3
  • 74
    • 0037805689 scopus 로고    scopus 로고
    • Regulation of p70 S6 kinase by complex formation between the Rac guanine nucleotide exchange factor (Rac-GEF) Tiam1 and the scaffold spinophilin
    • Buchsbaum R.J., Connolly B.A., Feig L.A. Regulation of p70 S6 kinase by complex formation between the Rac guanine nucleotide exchange factor (Rac-GEF) Tiam1 and the scaffold spinophilin. J. Biol. Chem. 2003, 278:18833-18841.
    • (2003) J. Biol. Chem. , vol.278 , pp. 18833-18841
    • Buchsbaum, R.J.1    Connolly, B.A.2    Feig, L.A.3
  • 76
    • 0033376412 scopus 로고    scopus 로고
    • Activity-dependent interaction of the intracellular domain of rat trkA with intermediate filament proteins, the beta-6 proteasomal subunit, Ras-GRF1, and the p162 subunit of eIF3
    • MacDonald J.I., Verdi J.M., Meakin S.O. Activity-dependent interaction of the intracellular domain of rat trkA with intermediate filament proteins, the beta-6 proteasomal subunit, Ras-GRF1, and the p162 subunit of eIF3. J. Mol. Neurosci. 1999, 13:141-158.
    • (1999) J. Mol. Neurosci. , vol.13 , pp. 141-158
    • MacDonald, J.I.1    Verdi, J.M.2    Meakin, S.O.3
  • 77
    • 12844256397 scopus 로고    scopus 로고
    • Neurotrophin-dependent tyrosine phosphorylation of Ras guanine-releasing factor 1 and associated neurite outgrowth is dependent on the HIKE domain of TrkA
    • Robinson K.N., Manto K., Buchsbaum R.J., MacDonald J.I., Meakin S.O. Neurotrophin-dependent tyrosine phosphorylation of Ras guanine-releasing factor 1 and associated neurite outgrowth is dependent on the HIKE domain of TrkA. J. Biol. Chem. 2005, 280:225-235.
    • (2005) J. Biol. Chem. , vol.280 , pp. 225-235
    • Robinson, K.N.1    Manto, K.2    Buchsbaum, R.J.3    MacDonald, J.I.4    Meakin, S.O.5
  • 78
    • 0027422977 scopus 로고
    • A coiled-coil oligomerization domain of Bcr is essential for the transforming function of Bcr-Abl oncoproteins
    • McWhirter J.R., Galasso D.L., Wang J.Y. A coiled-coil oligomerization domain of Bcr is essential for the transforming function of Bcr-Abl oncoproteins. Mol. Cell. Biol. 1993, 13:7587-7595.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 7587-7595
    • McWhirter, J.R.1    Galasso, D.L.2    Wang, J.Y.3
  • 79
    • 20444371580 scopus 로고    scopus 로고
    • Solution structure of the symmetric coiled coil tetramer formed by the oligomerization domain of hnRNP C: implications for biological function
    • Whitson S.R., LeStourgeon W.M., Krezel A.M. Solution structure of the symmetric coiled coil tetramer formed by the oligomerization domain of hnRNP C: implications for biological function. J. Mol. Biol. 2005, 350:319-337.
    • (2005) J. Mol. Biol. , vol.350 , pp. 319-337
    • Whitson, S.R.1    LeStourgeon, W.M.2    Krezel, A.M.3
  • 80
    • 0037138403 scopus 로고    scopus 로고
    • Calmodulin signaling via the IQ motif
    • Bahler M., Rhoads A. Calmodulin signaling via the IQ motif. FEBS Lett. 2002, 513:107-113.
    • (2002) FEBS Lett. , vol.513 , pp. 107-113
    • Bahler, M.1    Rhoads, A.2
  • 82
    • 0034038194 scopus 로고    scopus 로고
    • Calmodulin-independent coordination of Ras and extracellular signal-regulated kinase activation by Ras-GRF2
    • de Hoog C.L., Fan W.-T., Goldstein M.D., Moran M.F., Koch C.A. Calmodulin-independent coordination of Ras and extracellular signal-regulated kinase activation by Ras-GRF2. Mol. Cell. Biol. 2000, 20:2727-2733.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 2727-2733
    • de Hoog, C.L.1    Fan, W.-T.2    Goldstein, M.D.3    Moran, M.F.4    Koch, C.A.5
  • 83
    • 13444252631 scopus 로고    scopus 로고
    • GEF means go: turning on RHO GTPases with guanine nucleotide-exchange factors
    • Rossman K.L., Der C.J., 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    Der, C.J.2    Sondek, J.3
  • 85
    • 33646241782 scopus 로고    scopus 로고
    • The guanine nucleotide exchange factor RasGRF1 directly binds microtubules via DHPH2-mediated interaction
    • Forlani G., Baldassa S., Lavagni P., Sturani E., Zippel R. The guanine nucleotide exchange factor RasGRF1 directly binds microtubules via DHPH2-mediated interaction. FEBS J. 2006, 273:2127-2138.
    • (2006) FEBS J. , vol.273 , pp. 2127-2138
    • Forlani, G.1    Baldassa, S.2    Lavagni, P.3    Sturani, E.4    Zippel, R.5
  • 86
    • 34047253948 scopus 로고    scopus 로고
    • SCLIP, a microtubule-destabilizing factor, interacts with RasGRF1 and inhibits its ability to promote Rac activation and neurite outgrowth
    • Baldassa S., Gnesutta N., Fascio U., Sturani E., Zippel R. SCLIP, a microtubule-destabilizing factor, interacts with RasGRF1 and inhibits its ability to promote Rac activation and neurite outgrowth. J. Biol. Chem. 2007, 282:2333-2345.
    • (2007) J. Biol. Chem. , vol.282 , pp. 2333-2345
    • Baldassa, S.1    Gnesutta, N.2    Fascio, U.3    Sturani, E.4    Zippel, R.5
  • 87
    • 0030855008 scopus 로고    scopus 로고
    • Dimerization of Cdc25p, the guanine-nucleotide exchange factor for Ras from Saccharomyces cerevisiae, and its interaction with Sdc25p
    • Camus C., Geymonat M., Garreau H., Baudet-Nessler S., Jacquet M. Dimerization of Cdc25p, the guanine-nucleotide exchange factor for Ras from Saccharomyces cerevisiae, and its interaction with Sdc25p. Eur. J. Biochem. FEBS 1997, 247:703-708.
    • (1997) Eur. J. Biochem. FEBS , vol.247 , pp. 703-708
    • Camus, C.1    Geymonat, M.2    Garreau, H.3    Baudet-Nessler, S.4    Jacquet, M.5
  • 88
    • 0033917114 scopus 로고    scopus 로고
    • Immunoreceptor tyrosine-based inhibitory motifs on activating molecules
    • Sinclair N.R. Immunoreceptor tyrosine-based inhibitory motifs on activating molecules. Crit. Rev. Immunol. 2000, 20:89-102.
    • (2000) Crit. Rev. Immunol. , vol.20 , pp. 89-102
    • Sinclair, N.R.1
  • 89
    • 0027502176 scopus 로고
    • Influence of guanine nucleotides on complex formation between Ras and CDC25 proteins
    • Lai C.-C., Boguski M., Broek D., Powers S. Influence of guanine nucleotides on complex formation between Ras and CDC25 proteins. Mol. Cell. Biol. 1993, 13:1345-1352.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 1345-1352
    • Lai, C.-C.1    Boguski, M.2    Broek, D.3    Powers, S.4
  • 91
    • 0022971952 scopus 로고
    • Amino acid sequences common to rapidly degraded proteins: the PEST hypothesis
    • Rogers S., Wells R., Rechsteiner M. Amino acid sequences common to rapidly degraded proteins: the PEST hypothesis. Science 1986, 234:364-368.
    • (1986) Science , vol.234 , pp. 364-368
    • Rogers, S.1    Wells, R.2    Rechsteiner, M.3
  • 93
    • 0033601374 scopus 로고    scopus 로고
    • Phosphorylation of serine 916 of Ras-GRF1 contributes to the activation of exchange factor activity by muscarinic receptors
    • Mattingly R.R. Phosphorylation of serine 916 of Ras-GRF1 contributes to the activation of exchange factor activity by muscarinic receptors. J. Biol. Chem. 1999, 274:37379-37384.
    • (1999) J. Biol. Chem. , vol.274 , pp. 37379-37384
    • Mattingly, R.R.1
  • 95
    • 0036364408 scopus 로고    scopus 로고
    • A growing family of guanine nucleotide exchange factors is responsible for activation of Ras-family GTPases
    • Quilliam L.A., Rebhun J.F., Castro A.F. A growing family of guanine nucleotide exchange factors is responsible for activation of Ras-family GTPases. Prog. Nucleic Acid Res. Mol. Biol. 2002, 71:391-444.
    • (2002) Prog. Nucleic Acid Res. Mol. Biol. , vol.71 , pp. 391-444
    • Quilliam, L.A.1    Rebhun, J.F.2    Castro, A.F.3
  • 96
    • 28844438376 scopus 로고    scopus 로고
    • The isolated catalytic hairpin of the Ras-specific guanine nucleotide exchange factor Cdc25Mm retains nucleotide dissociation activity but has impaired nucleotide exchange activity
    • Sacco E., Fantinato S., Manzoni R., Metalli D., De Gioia L., Fantucci P., Alberghina L., Vanoni M. The isolated catalytic hairpin of the Ras-specific guanine nucleotide exchange factor Cdc25Mm retains nucleotide dissociation activity but has impaired nucleotide exchange activity. FEBS Lett. 2005, 579:6851-6858.
    • (2005) FEBS Lett. , vol.579 , pp. 6851-6858
    • Sacco, E.1    Fantinato, S.2    Manzoni, R.3    Metalli, D.4    De Gioia, L.5    Fantucci, P.6    Alberghina, L.7    Vanoni, M.8
  • 98
    • 58149187996 scopus 로고    scopus 로고
    • Differences in flexibility underlie functional differences in the Ras activators son of sevenless and Ras guanine nucleotide releasing factor 1
    • Freedman T.S., Sondermann H., Kuchment O., Friedland G.D., Kortemme T., Kuriyan J. Differences in flexibility underlie functional differences in the Ras activators son of sevenless and Ras guanine nucleotide releasing factor 1. Structure 2009, 17:41-53.
    • (2009) Structure , vol.17 , pp. 41-53
    • Freedman, T.S.1    Sondermann, H.2    Kuchment, O.3    Friedland, G.D.4    Kortemme, T.5    Kuriyan, J.6
  • 99
    • 0032538316 scopus 로고    scopus 로고
    • Crystal structure of the Dbl and pleckstrin homology domains from the human Son of sevenless protein
    • Soisson S.M., Nimnual A.S., Uy M., Bar-Sagi D., Kuriyan J. Crystal structure of the Dbl and pleckstrin homology domains from the human Son of sevenless protein. Cell 1998, 95:259-268.
    • (1998) Cell , vol.95 , pp. 259-268
    • Soisson, S.M.1    Nimnual, A.S.2    Uy, M.3    Bar-Sagi, D.4    Kuriyan, J.5
  • 100
    • 0345528059 scopus 로고    scopus 로고
    • Tandem histone folds in the structure of the N-terminal segment of the ras activator Son of Sevenless
    • Sondermann H., Soisson S.M., Bar-Sagi D., Kuriyan J. Tandem histone folds in the structure of the N-terminal segment of the ras activator Son of Sevenless. Structure 2003, 11:1583-1593.
    • (2003) Structure , vol.11 , pp. 1583-1593
    • Sondermann, H.1    Soisson, S.M.2    Bar-Sagi, D.3    Kuriyan, J.4
  • 103
    • 0032473829 scopus 로고    scopus 로고
    • Analysis of the secondary structure of the catalytic domain of mouse Ras exchange factor CDC25Mm
    • Coccetti P., Monzani E., Alberghina L., Casella L., Martegani E. Analysis of the secondary structure of the catalytic domain of mouse Ras exchange factor CDC25Mm. Biochim. Biophys. Acta 1998, 1383:292-300.
    • (1998) Biochim. Biophys. Acta , vol.1383 , pp. 292-300
    • Coccetti, P.1    Monzani, E.2    Alberghina, L.3    Casella, L.4    Martegani, E.5
  • 104
    • 0142063443 scopus 로고    scopus 로고
    • Structure determination and dynamics of peptides overlapping the catalytic hairpin of the Ras-specific GEF Cdc25(Mm)
    • Consonni R., Arosio I., Recca T., Longhi R., Colombo G., Vanoni M. Structure determination and dynamics of peptides overlapping the catalytic hairpin of the Ras-specific GEF Cdc25(Mm). Biochemistry 2003, 42:12154-12162.
    • (2003) Biochemistry , vol.42 , pp. 12154-12162
    • Consonni, R.1    Arosio, I.2    Recca, T.3    Longhi, R.4    Colombo, G.5    Vanoni, M.6
  • 105
    • 0035851150 scopus 로고    scopus 로고
    • Prenylation of target GTPases contributes to signaling specificity of Ras-guanine nucleotide exchange factors
    • Gotoh T., Tian X., Feig L.A. Prenylation of target GTPases contributes to signaling specificity of Ras-guanine nucleotide exchange factors. J. Biol. Chem. 2001, 276:38029-38035.
    • (2001) J. Biol. Chem. , vol.276 , pp. 38029-38035
    • Gotoh, T.1    Tian, X.2    Feig, L.A.3
  • 106
    • 0035861736 scopus 로고    scopus 로고
    • Basis for signaling specificity difference between Sos and Ras-GRF guanine nucleotide exchange factors
    • Tian X., Feig L.A. Basis for signaling specificity difference between Sos and Ras-GRF guanine nucleotide exchange factors. J. Biol. Chem. 2001, 276:47248-47256.
    • (2001) J. Biol. Chem. , vol.276 , pp. 47248-47256
    • Tian, X.1    Feig, L.A.2
  • 108
    • 0031917171 scopus 로고    scopus 로고
    • Ras-GRF activates Ha-Ras, but not N-Ras or K-Ras 4B, protein in vivo
    • Jones M.K., Jackson J.H. Ras-GRF activates Ha-Ras, but not N-Ras or K-Ras 4B, protein in vivo. J. Biol. Chem. 1998, 273:1782-1787.
    • (1998) J. Biol. Chem. , vol.273 , pp. 1782-1787
    • Jones, M.K.1    Jackson, J.H.2
  • 111
    • 0033592703 scopus 로고    scopus 로고
    • Signal transduction elements of TC21, an oncogenic member of the R-Ras subfamily of GTP-binding proteins
    • Movilla N., Crespo P., Bustelo X.R. Signal transduction elements of TC21, an oncogenic member of the R-Ras subfamily of GTP-binding proteins. Oncogene 1999, 18:5860-5869.
    • (1999) Oncogene , vol.18 , pp. 5860-5869
    • Movilla, N.1    Crespo, P.2    Bustelo, X.R.3
  • 113
    • 0033588299 scopus 로고    scopus 로고
    • M-Ras/R-Ras3, a transforming Ras protein regulated by Sos1, GRF1, and p120 Ras GTPase-activating protein, interacts with the putative Ras effector AF6
    • Quilliam L.A., Castro A.F., Rogers-Graham K.S., Martin C.B., Der C.J., Bi C. M-Ras/R-Ras3, a transforming Ras protein regulated by Sos1, GRF1, and p120 Ras GTPase-activating protein, interacts with the putative Ras effector AF6. J. Biol. Chem. 1999, 274:23850-23857.
    • (1999) J. Biol. Chem. , vol.274 , pp. 23850-23857
    • Quilliam, L.A.1    Castro, A.F.2    Rogers-Graham, K.S.3    Martin, C.B.4    Der, C.J.5    Bi, C.6
  • 114
    • 70350098086 scopus 로고    scopus 로고
    • Structural and spatial determinants regulating TC21 activation by RasGRF family nucleotide exchange factors
    • Calvo F., Crespo P. Structural and spatial determinants regulating TC21 activation by RasGRF family nucleotide exchange factors. Mol. Biol. Cell 2009, 20:4289-4302.
    • (2009) Mol. Biol. Cell , vol.20 , pp. 4289-4302
    • Calvo, F.1    Crespo, P.2
  • 115
    • 0034008403 scopus 로고    scopus 로고
    • Induction of rac-guanine nucleotide exchange activity of Ras-GRF1/CDC25(Mm) following phosphorylation by the nonreceptor tyrosine kinase Src
    • Kiyono M., Kaziro Y., Satoh T. Induction of rac-guanine nucleotide exchange activity of Ras-GRF1/CDC25(Mm) following phosphorylation by the nonreceptor tyrosine kinase Src. J. Biol. Chem. 2000, 275:5441-5446.
    • (2000) J. Biol. Chem. , vol.275 , pp. 5441-5446
    • Kiyono, M.1    Kaziro, Y.2    Satoh, T.3
  • 117
    • 61749103498 scopus 로고    scopus 로고
    • Ras subcellular localization defines extracellular signal-regulated kinase 1 and 2 substrate specificity through distinct utilization of scaffold proteins
    • Casar B., Arozarena I., Sanz-Moreno V., Pinto A., Agudo-Ibanez L., Marais R., Lewis R.E., Berciano M.T., Crespo P. Ras subcellular localization defines extracellular signal-regulated kinase 1 and 2 substrate specificity through distinct utilization of scaffold proteins. Mol. Cell. Biol. 2009, 29:1338-1353.
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 1338-1353
    • Casar, B.1    Arozarena, I.2    Sanz-Moreno, V.3    Pinto, A.4    Agudo-Ibanez, L.5    Marais, R.6    Lewis, R.E.7    Berciano, M.T.8    Crespo, P.9
  • 118
    • 0034705227 scopus 로고    scopus 로고
    • Scaffold proteins may biphasically affect the levels of mitogen-activated protein kinase signaling and reduce its threshold properties
    • Levchenko A., Bruck J., Sternberg P.W. Scaffold proteins may biphasically affect the levels of mitogen-activated protein kinase signaling and reduce its threshold properties. Proc. Natl Acad. Sci. USA 2000, 97:5818-5823.
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 5818-5823
    • Levchenko, A.1    Bruck, J.2    Sternberg, P.W.3
  • 119
    • 22744432389 scopus 로고    scopus 로고
    • Scaffold proteins dictate Rho GTPase-signaling specificity
    • Marinissen M.J., Gutkind J.S. Scaffold proteins dictate Rho GTPase-signaling specificity. Trends Biochem. Sci. 2005, 30:423-426.
    • (2005) Trends Biochem. Sci. , vol.30 , pp. 423-426
    • Marinissen, M.J.1    Gutkind, J.S.2
  • 120
    • 0033458830 scopus 로고    scopus 로고
    • Targeting of PKA, PKC and protein phosphatases to cellular microdomains
    • Sim A.T., Scott J.D. Targeting of PKA, PKC and protein phosphatases to cellular microdomains. Cell Calcium 1999, 26:209-217.
    • (1999) Cell Calcium , vol.26 , pp. 209-217
    • Sim, A.T.1    Scott, J.D.2
  • 121
    • 13944278759 scopus 로고    scopus 로고
    • Calmodulin-dependent kinase kinase/calmodulin kinase I activity gates extracellular-regulated kinase-dependent long-term potentiation
    • Schmitt J.M., Guire E.S., Saneyoshi T., Soderling T.R. Calmodulin-dependent kinase kinase/calmodulin kinase I activity gates extracellular-regulated kinase-dependent long-term potentiation. J. Neurosci. 2005, 25:1281-1290.
    • (2005) J. Neurosci. , vol.25 , pp. 1281-1290
    • Schmitt, J.M.1    Guire, E.S.2    Saneyoshi, T.3    Soderling, T.R.4
  • 122
    • 77955379103 scopus 로고    scopus 로고
    • Long-term potentiation in the CA1 hippocampus induced by NR2A subunit-containing NMDA glutamate receptors is mediated by Ras-GRF2/Erk map kinase signaling
    • Jin S.X., Feig L.A. Long-term potentiation in the CA1 hippocampus induced by NR2A subunit-containing NMDA glutamate receptors is mediated by Ras-GRF2/Erk map kinase signaling. PLoS ONE 2010, 5:e11732.
    • (2010) PLoS ONE , vol.5
    • Jin, S.X.1    Feig, L.A.2
  • 123
    • 33646378915 scopus 로고    scopus 로고
    • Age-dependent participation of Ras-GRF proteins in coupling calcium-permeable AMPA glutamate receptors to Ras/Erk signaling in cortical neurons
    • Tian X., Feig L.A. Age-dependent participation of Ras-GRF proteins in coupling calcium-permeable AMPA glutamate receptors to Ras/Erk signaling in cortical neurons. J. Biol. Chem. 2006, 281:7578-7582.
    • (2006) J. Biol. Chem. , vol.281 , pp. 7578-7582
    • Tian, X.1    Feig, L.A.2
  • 124
    • 18444415156 scopus 로고    scopus 로고
    • Endogenous expression and protein kinase A-dependent phosphorylation of the guanine nucleotide exchange factor Ras-GRF1 in human embryonic kidney 293 cells
    • Norum J.H., Methi T., Mattingly R.R., Levy F.O. Endogenous expression and protein kinase A-dependent phosphorylation of the guanine nucleotide exchange factor Ras-GRF1 in human embryonic kidney 293 cells. FEBS J. 2005, 272:2304-2316.
    • (2005) FEBS J. , vol.272 , pp. 2304-2316
    • Norum, J.H.1    Methi, T.2    Mattingly, R.R.3    Levy, F.O.4
  • 125
    • 24344508124 scopus 로고    scopus 로고
    • Calcium-activated RAF/MEK/ERK signaling pathway mediates p53-dependent apoptosis and is abrogated by alpha B-crystallin through inhibition of RAS activation
    • Li D.W., Liu J.P., Mao Y.W., Xiang H., Wang J., Ma W.Y., Dong Z., Pike H.M., Brown R.E., Reed J.C. Calcium-activated RAF/MEK/ERK signaling pathway mediates p53-dependent apoptosis and is abrogated by alpha B-crystallin through inhibition of RAS activation. Mol. Biol. Cell 2005, 16:4437-4453.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 4437-4453
    • Li, D.W.1    Liu, J.P.2    Mao, Y.W.3    Xiang, H.4    Wang, J.5    Ma, W.Y.6    Dong, Z.7    Pike, H.M.8    Brown, R.E.9    Reed, J.C.10
  • 127
    • 70450263435 scopus 로고    scopus 로고
    • Fine-tuning of GPCR activity by receptor-interacting proteins
    • Ritter S.L., Hall R.A. Fine-tuning of GPCR activity by receptor-interacting proteins. Nat. Rev. Mol. Cell Biol. 2009, 10:819-830.
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 819-830
    • Ritter, S.L.1    Hall, R.A.2
  • 128
    • 0029017628 scopus 로고
    • Differential response of the Ras exchange factor, Ras-GRF to tyrosine kinase and G protein mediated signals
    • Shou C., Wurmser A., Ling K., Barbacid M., Feig L.A. Differential response of the Ras exchange factor, Ras-GRF to tyrosine kinase and G protein mediated signals. Oncogene 1995, 10:1887-1893.
    • (1995) Oncogene , vol.10 , pp. 1887-1893
    • Shou, C.1    Wurmser, A.2    Ling, K.3    Barbacid, M.4    Feig, L.A.5
  • 129
    • 0029884725 scopus 로고    scopus 로고
    • The brain specific Ras exchange factor CDC25 Mm: modulation of its activity through Gi-protein-mediated signals
    • Zippel R., Orecchia S., Sturani E., Martegani E. The brain specific Ras exchange factor CDC25 Mm: modulation of its activity through Gi-protein-mediated signals. Oncogene 1996, 12:2697-2703.
    • (1996) Oncogene , vol.12 , pp. 2697-2703
    • Zippel, R.1    Orecchia, S.2    Sturani, E.3    Martegani, E.4
  • 130
    • 0029664925 scopus 로고    scopus 로고
    • Phosphorylation-dependent activation of the Ras-GRF/CDC25Mm exchange factor by muscarinic receptors and G-protein beta gamma subunits
    • Mattingly R.R., Macara I.G. Phosphorylation-dependent activation of the Ras-GRF/CDC25Mm exchange factor by muscarinic receptors and G-protein beta gamma subunits. Nature 1996, 382:268-272.
    • (1996) Nature , vol.382 , pp. 268-272
    • Mattingly, R.R.1    Macara, I.G.2
  • 131
    • 0033057582 scopus 로고    scopus 로고
    • Activation of the Ras-GRF/CDC25Mm exchange factor by lysophosphatidic acid
    • Mattingly R.R., Saini V., Macara I.G. Activation of the Ras-GRF/CDC25Mm exchange factor by lysophosphatidic acid. Cell. Signal. 1999, 11:603-610.
    • (1999) Cell. Signal. , vol.11 , pp. 603-610
    • Mattingly, R.R.1    Saini, V.2    Macara, I.G.3
  • 132
    • 0037631371 scopus 로고    scopus 로고
    • Phosphorylation of the Ras-GRF1 exchange factor at Ser916/898 reveals activation of Ras signaling in the cerebral cortex
    • Yang H., Cooley D., Legakis J.E., Ge Q., Andrade R., Mattingly R.R. Phosphorylation of the Ras-GRF1 exchange factor at Ser916/898 reveals activation of Ras signaling in the cerebral cortex. J. Biol. Chem. 2003, 278:13278-13285.
    • (2003) J. Biol. Chem. , vol.278 , pp. 13278-13285
    • Yang, H.1    Cooley, D.2    Legakis, J.E.3    Ge, Q.4    Andrade, R.5    Mattingly, R.R.6
  • 133
    • 33845665020 scopus 로고    scopus 로고
    • Epac- and Rap-independent ERK1/2 phosphorylation induced by Gs-coupled receptor stimulation in HEK293 cells
    • Norum J.H., Dawood H., Mattingly R.R., Sandnes D., Levy F.O. Epac- and Rap-independent ERK1/2 phosphorylation induced by Gs-coupled receptor stimulation in HEK293 cells. FEBS Lett. 2007, 581:15-20.
    • (2007) FEBS Lett. , vol.581 , pp. 15-20
    • Norum, J.H.1    Dawood, H.2    Mattingly, R.R.3    Sandnes, D.4    Levy, F.O.5
  • 134
    • 62749198071 scopus 로고    scopus 로고
    • The rapid activation of N-Ras by alpha-thrombin in fibroblasts is mediated by the specific G-protein Galphai2-Gbeta1-Ggamma5 and occurs in lipid rafts
    • Lents N.H., Irintcheva V., Goel R., Wheeler L.W., Baldassare J.J. The rapid activation of N-Ras by alpha-thrombin in fibroblasts is mediated by the specific G-protein Galphai2-Gbeta1-Ggamma5 and occurs in lipid rafts. Cell. Signal. 2009, 21:1007-1014.
    • (2009) Cell. Signal. , vol.21 , pp. 1007-1014
    • Lents, N.H.1    Irintcheva, V.2    Goel, R.3    Wheeler, L.W.4    Baldassare, J.J.5
  • 135
    • 33745745744 scopus 로고    scopus 로고
    • The Ras-GRF1 exchange factor coordinates activation of H-Ras and Rac1 to control neuronal morphology
    • Yang H., Mattingly R.R. The Ras-GRF1 exchange factor coordinates activation of H-Ras and Rac1 to control neuronal morphology. Mol. Biol. Cell 2006, 17:2177-2189.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 2177-2189
    • Yang, H.1    Mattingly, R.R.2
  • 136
    • 0034839050 scopus 로고    scopus 로고
    • Differential actions of p60c-Src and Lck kinases on the Ras regulators p120-GAP and GDP/GTP exchange factor CDC25Mm
    • Giglione C., Gonfloni S., Parmeggiani A. Differential actions of p60c-Src and Lck kinases on the Ras regulators p120-GAP and GDP/GTP exchange factor CDC25Mm. Eur. J. Biochem. FEBS 2001, 268:3275-3283.
    • (2001) Eur. J. Biochem. FEBS , vol.268 , pp. 3275-3283
    • Giglione, C.1    Gonfloni, S.2    Parmeggiani, A.3
  • 137
    • 0034703005 scopus 로고    scopus 로고
    • Stimulation of Ras guanine nucleotide exchange activity of Ras-GRF1/CDC25(Mm) upon tyrosine phosphorylation by the Cdc42-regulated kinase ACK1
    • Kiyono M., Kato J., Kataoka T., Kaziro Y., Satoh T. Stimulation of Ras guanine nucleotide exchange activity of Ras-GRF1/CDC25(Mm) upon tyrosine phosphorylation by the Cdc42-regulated kinase ACK1. J. Biol. Chem. 2000, 275:29788-29793.
    • (2000) J. Biol. Chem. , vol.275 , pp. 29788-29793
    • Kiyono, M.1    Kato, J.2    Kataoka, T.3    Kaziro, Y.4    Satoh, T.5
  • 138
    • 0035877781 scopus 로고    scopus 로고
    • Maintenance of CDC42 GDP-bound state by Rho-GDI inhibits MAP kinase activation by the exchange factor Ras-GRF. evidence for Ras-GRF function being inhibited by Cdc42-GDP but unaffected by CDC42-GTP
    • Arozarena I., Matallanas D., Crespo P. Maintenance of CDC42 GDP-bound state by Rho-GDI inhibits MAP kinase activation by the exchange factor Ras-GRF. evidence for Ras-GRF function being inhibited by Cdc42-GDP but unaffected by CDC42-GTP. J. Biol. Chem. 2001, 276:21878-21884.
    • (2001) J. Biol. Chem. , vol.276 , pp. 21878-21884
    • Arozarena, I.1    Matallanas, D.2    Crespo, P.3
  • 139
    • 0036721009 scopus 로고    scopus 로고
    • Inhibitory effects of a dominant-interfering form of the Rho-GTPase Cdc42 in the chemoattractant-elicited signaling pathways leading to NADPH oxidase activation in differentiated HL-60 cells
    • Rabiet M.J., Tardif M., Braun L., Boulay F. Inhibitory effects of a dominant-interfering form of the Rho-GTPase Cdc42 in the chemoattractant-elicited signaling pathways leading to NADPH oxidase activation in differentiated HL-60 cells. Blood 2002, 100:1835-1844.
    • (2002) Blood , vol.100 , pp. 1835-1844
    • Rabiet, M.J.1    Tardif, M.2    Braun, L.3    Boulay, F.4
  • 141
    • 0027999033 scopus 로고
    • Membrane-targeting potentiates guanine nucleotide exchange factor CDC25 and SOS1 activation of Ras transforming activity
    • Quilliam L.A., Huff S.Y., Rabun K.M., Wei W., Park W., Broek D., Der C.J. Membrane-targeting potentiates guanine nucleotide exchange factor CDC25 and SOS1 activation of Ras transforming activity. Proc. Natl Acad. Sci. USA 1994, 91:8512-8516.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 8512-8516
    • Quilliam, L.A.1    Huff, S.Y.2    Rabun, K.M.3    Wei, W.4    Park, W.5    Broek, D.6    Der, C.J.7
  • 142
    • 0033008732 scopus 로고    scopus 로고
    • Expression of Ras-GRF in the SK-N-BE neuroblastoma accelerates retinoic-acid-induced neuronal differentiation and increases the functional expression of the IRK1 potassium channel
    • Tonini R., Mancinelli E., Balestrini M., Mazzanti M., Martegani E., Ferroni A., Sturani E., Zippel R. Expression of Ras-GRF in the SK-N-BE neuroblastoma accelerates retinoic-acid-induced neuronal differentiation and increases the functional expression of the IRK1 potassium channel. Eur. J. Neurosci. 1999, 11:959-966.
    • (1999) Eur. J. Neurosci. , vol.11 , pp. 959-966
    • Tonini, R.1    Mancinelli, E.2    Balestrini, M.3    Mazzanti, M.4    Martegani, E.5    Ferroni, A.6    Sturani, E.7    Zippel, R.8
  • 145
    • 34250754825 scopus 로고    scopus 로고
    • Haloperidol induces neurotoxicity by the NMDA receptor downstream signaling pathway, alternative from glutamate excitotoxicity
    • Zhuravliova E., Barbakadze T., Natsvlishvili N., Mikeladze D.G. Haloperidol induces neurotoxicity by the NMDA receptor downstream signaling pathway, alternative from glutamate excitotoxicity. Neurochem. Int. 2007, 50:976-982.
    • (2007) Neurochem. Int. , vol.50 , pp. 976-982
    • Zhuravliova, E.1    Barbakadze, T.2    Natsvlishvili, N.3    Mikeladze, D.G.4
  • 146
    • 18844399321 scopus 로고    scopus 로고
    • Ras/ERK signalling in cannabinoid tolerance: from behaviour to cellular aspects
    • Rubino T., Forlani G., Vigano D., Zippel R., Parolaro D. Ras/ERK signalling in cannabinoid tolerance: from behaviour to cellular aspects. J. Neurochem. 2005, 93:984-991.
    • (2005) J. Neurochem. , vol.93 , pp. 984-991
    • Rubino, T.1    Forlani, G.2    Vigano, D.3    Zippel, R.4    Parolaro, D.5
  • 147
    • 33747838016 scopus 로고    scopus 로고
    • Changes in the expression of G protein-coupled receptor kinases and beta-arrestins in mouse brain during cannabinoid tolerance: a role for RAS-ERK cascade
    • Rubino T., Vigano D., Premoli F., Castiglioni C., Bianchessi S., Zippel R., Parolaro D. Changes in the expression of G protein-coupled receptor kinases and beta-arrestins in mouse brain during cannabinoid tolerance: a role for RAS-ERK cascade. Mol. Neurobiol. 2006, 33:199-213.
    • (2006) Mol. Neurobiol. , vol.33 , pp. 199-213
    • Rubino, T.1    Vigano, D.2    Premoli, F.3    Castiglioni, C.4    Bianchessi, S.5    Zippel, R.6    Parolaro, D.7
  • 148
    • 33744980677 scopus 로고    scopus 로고
    • ERK-dependent modulation of cerebellar synaptic plasticity after chronic Delta9-tetrahydrocannabinol exposure
    • Tonini R., Ciardo S., Cerovic M., Rubino T., Parolaro D., Mazzanti M., Zippel R. ERK-dependent modulation of cerebellar synaptic plasticity after chronic Delta9-tetrahydrocannabinol exposure. J. Neurosci. 2006, 26:5810-5818.
    • (2006) J. Neurosci. , vol.26 , pp. 5810-5818
    • Tonini, R.1    Ciardo, S.2    Cerovic, M.3    Rubino, T.4    Parolaro, D.5    Mazzanti, M.6    Zippel, R.7
  • 150
    • 33645734748 scopus 로고    scopus 로고
    • Effect of transforming growth factor-beta on decorin and beta1 integrin expression during muscle development in chickens
    • Li X., McFarland D.C., Velleman S.G. Effect of transforming growth factor-beta on decorin and beta1 integrin expression during muscle development in chickens. Poult. Sci. 2006, 85:326-332.
    • (2006) Poult. Sci. , vol.85 , pp. 326-332
    • Li, X.1    McFarland, D.C.2    Velleman, S.G.3
  • 151
  • 153
    • 0037468270 scopus 로고    scopus 로고
    • Allelic imbalance and altered expression of genes in chromosome 2q11-2q16 from rat mammary gland carcinomas induced by 2-amino-1-methyl-6-phenylimidazo[4, 5-b]pyridine
    • Qiu C., Yu M., Shan L., Snyderwine E.G. Allelic imbalance and altered expression of genes in chromosome 2q11-2q16 from rat mammary gland carcinomas induced by 2-amino-1-methyl-6-phenylimidazo[4, 5-b]pyridine. Oncogene 2003, 22:1253-1260.
    • (2003) Oncogene , vol.22 , pp. 1253-1260
    • Qiu, C.1    Yu, M.2    Shan, L.3    Snyderwine, E.G.4
  • 155
  • 156
    • 1642315483 scopus 로고    scopus 로고
    • Modulation of extracellular signal-regulated kinases cascade by chronic delta 9-tetrahydrocannabinol treatment
    • Rubino T., Forlani G., Vigano D., Zippel R., Parolaro D. Modulation of extracellular signal-regulated kinases cascade by chronic delta 9-tetrahydrocannabinol treatment. Mol. Cell. Neurosci. 2004, 25:355-362.
    • (2004) Mol. Cell. Neurosci. , vol.25 , pp. 355-362
    • Rubino, T.1    Forlani, G.2    Vigano, D.3    Zippel, R.4    Parolaro, D.5
  • 157
    • 34247486969 scopus 로고    scopus 로고
    • Laser microdissection and microarray analysis of the hippocampus of Ras-GRF1 knockout mice reveals gene expression changes affecting signal transduction pathways related to memory and learning
    • Fernandez-Medarde A., Porteros A., de Las Rivas J., Nunez A., Fuster J.J., Santos E. Laser microdissection and microarray analysis of the hippocampus of Ras-GRF1 knockout mice reveals gene expression changes affecting signal transduction pathways related to memory and learning. Neuroscience 2007, 146:272-285.
    • (2007) Neuroscience , vol.146 , pp. 272-285
    • Fernandez-Medarde, A.1    Porteros, A.2    de Las Rivas, J.3    Nunez, A.4    Fuster, J.J.5    Santos, E.6
  • 158
    • 0037452986 scopus 로고    scopus 로고
    • Pituitary tumor transforming gene-null male mice exhibit impaired pancreatic beta cell proliferation and diabetes
    • Wang Z., Moro E., Kovacs K., Yu R., Melmed S. Pituitary tumor transforming gene-null male mice exhibit impaired pancreatic beta cell proliferation and diabetes. Proc. Natl Acad. Sci. USA 2003, 100:3428-3432.
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 3428-3432
    • Wang, Z.1    Moro, E.2    Kovacs, K.3    Yu, R.4    Melmed, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.