메뉴 건너뛰기




Volumn 17, Issue 5, 2006, Pages 2177-2189

The Ras-GRF1 exchange factor coordinates activation of H-Ras and Rac1 to control neuronal morphology

Author keywords

[No Author keywords available]

Indexed keywords

GUANINE NUCLEOTIDE EXCHANGE FACTOR; GUANOSINE TRIPHOSPHATE; MITOGEN ACTIVATED PROTEIN KINASE; PROTEIN GRF1; PROTEIN H RAS; PROTEIN KINASE B; RAC1 PROTEIN; RAS PROTEIN; RHOA GUANINE NUCLEOTIDE BINDING PROTEIN; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG; WORTMANNIN;

EID: 33745745744     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E05-10-0913     Document Type: Article
Times cited : (26)

References (81)
  • 1
    • 3042604615 scopus 로고    scopus 로고
    • Neuronal activation of Ras regulates synaptic connectivity
    • Arendt, T. et al. (2004). Neuronal activation of Ras regulates synaptic connectivity. Eur. J. Neurosci. 19, 2953-2966.
    • (2004) Eur. J. Neurosci. , vol.19 , pp. 2953-2966
    • Arendt, T.1
  • 3
    • 0035836791 scopus 로고    scopus 로고
    • Rho signals to cell growth and apoptosis
    • Aznar, S., and Lacal, J. C. (2001). Rho signals to cell growth and apoptosis. Cancer Lett. 365, 1-10.
    • (2001) Cancer Lett. , vol.365 , pp. 1-10
    • Aznar, S.1    Lacal, J.C.2
  • 4
    • 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., and Parmeggiani, A. (1997). 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. 272, 6671-6676.
    • (1997) J. Biol. Chem. , vol.272 , pp. 6671-6676
    • Baouz, S.1    Jacquet, E.2    Bernardi, A.3    Parmeggiani, A.4
  • 5
    • 0022137480 scopus 로고
    • Microinjection of the Ras oncogene protein into PC12 cells induces morphological differentiation
    • Bar-Sagi, D., and Feramisco, J. R. (1985). Microinjection of the Ras oncogene protein into PC12 cells induces morphological differentiation. Cell 42, 841-848.
    • (1985) Cell , vol.42 , pp. 841-848
    • Bar-Sagi, D.1    Feramisco, J.R.2
  • 7
    • 0037018153 scopus 로고    scopus 로고
    • High RhoA activity maintains the undifferentiated mesenchymal cell phenotype, whereas RhoA down-regulation by laminin-2 induces smooth muscle myogenesis
    • Beqaj, S., Jakkaraju, S., Mattingly, R. R., Pan, D., and Schuger, L. (2002). High RhoA activity maintains the undifferentiated mesenchymal cell phenotype, whereas RhoA down-regulation by laminin-2 induces smooth muscle myogenesis. J. Cell Biol. 156, 893-903.
    • (2002) J. Cell Biol. , vol.156 , pp. 893-903
    • Beqaj, S.1    Jakkaraju, S.2    Mattingly, R.R.3    Pan, D.4    Schuger, L.5
  • 8
    • 3042796979 scopus 로고    scopus 로고
    • GAP control: Regulating the regulators of small GTPases
    • Bernards, A., and Settleman, J. (2004). GAP control: regulating the regulators of small GTPases. Trends Cell Biol. 24, 377-385.
    • (2004) Trends Cell Biol. , vol.24 , pp. 377-385
    • Bernards, A.1    Settleman, J.2
  • 9
    • 0027732538 scopus 로고
    • Proteins regulating Ras and its relatives
    • Boguski, M. S., and McCormick, F. (1993). Proteins regulating Ras and its relatives. Nature 366, 643-654.
    • (1993) Nature , vol.366 , pp. 643-654
    • Boguski, M.S.1    McCormick, F.2
  • 10
    • 0031581209 scopus 로고    scopus 로고
    • A role for the Ras signalling pathway in synaptic transmission and long-term memory
    • Brambilla, R. et al. (1997). A role for the Ras signalling pathway in synaptic transmission and long-term memory. Nature 390, 281-286.
    • (1997) Nature , vol.390 , pp. 281-286
    • Brambilla, R.1
  • 12
    • 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., and Feig, L. A. (2002). Interaction of Rac exchange factors Tiam1 and Ras-GRF1 with a scaffold for the p38 mitogen-activated protein kinase cascade. Mol. Cell. Biol. 22, 4073-4085.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 4073-4085
    • Buchsbaum, R.J.1    Connolly, B.A.2    Feig, L.A.3
  • 13
    • 0029899120 scopus 로고    scopus 로고
    • Evidence using a green fluorescent protein-glucocorticoid receptor chimera that the Ran/TC4 GTPase mediates an essential function independent of nuclear protein import
    • Carey, K. L., Richards, S. A., Lounsbury, K. M., and Macara, I. G. (1996). Evidence using a green fluorescent protein-glucocorticoid receptor chimera that the Ran/TC4 GTPase mediates an essential function independent of nuclear protein import. J. Cell Biol. 233, 985-996.
    • (1996) J. Cell Biol. , vol.233 , pp. 985-996
    • Carey, K.L.1    Richards, S.A.2    Lounsbury, K.M.3    Macara, I.G.4
  • 14
    • 15944369335 scopus 로고    scopus 로고
    • Spine architecture and synaptic plasticity
    • Carlisle, H. J., and Kennedy, M. B. (2005). Spine architecture and synaptic plasticity. Trends Neurosci. 28, 182-187.
    • (2005) Trends Neurosci. , vol.28 , pp. 182-187
    • Carlisle, H.J.1    Kennedy, M.B.2
  • 15
    • 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., and Lowy, D. R. (1993). Regulated and constitutive activity by CDC25Mm (GRF), a Ras-specific exchange factor. Mol. Cell. Biol. 23, 7718-7724.
    • (1993) Mol. Cell. Biol. , vol.23 , pp. 7718-7724
    • Cen, H.1    Papageorge, A.G.2    Vass, W.C.3    Zhang, K.E.4    Lowy, D.R.5
  • 16
    • 0032472918 scopus 로고    scopus 로고
    • Membrane targeting of p21-activated kinase 1 (PAK1) induces neurite outgrowth from PC12 cells
    • Daniels, R. H., Hall, P. S., and Bokoch, G. M. (1998). Membrane targeting of p21-activated kinase 1 (PAK1) induces neurite outgrowth from PC12 cells. EMBO J. 27, 754-764.
    • (1998) EMBO J. , vol.27 , pp. 754-764
    • Daniels, R.H.1    Hall, P.S.2    Bokoch, G.M.3
  • 17
    • 0025790437 scopus 로고
    • Identification and characterization of the neurofibromatosis type 1 protein product
    • DeClue, J. E., Cohen, B. D., and Lowy, D. R. (1991). Identification and characterization of the neurofibromatosis type 1 protein product. Proc. Natl. Acad. Sci. USA 88, 9914-9918.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 9914-9918
    • DeClue, J.E.1    Cohen, B.D.2    Lowy, D.R.3
  • 19
    • 0034788432 scopus 로고    scopus 로고
    • Hippocampus-dependent learning and memory is impaired in mice lacking the Ras-guanine-nucleotide releasing factor 1 (Ras-GRF1)
    • Giese, K. P., Friedman, E., Telliez, J. B., Fedorov, N. B., Wines, M., Feig, L. A., and Silva, A. J. (2001). Hippocampus-dependent learning and memory is impaired in mice lacking the Ras-guanine-nucleotide releasing factor 1 (Ras-GRF1). Neuropharmacology 41, 791-800.
    • (2001) Neuropharmacology , vol.41 , pp. 791-800
    • Giese, K.P.1    Friedman, E.2    Telliez, J.B.3    Fedorov, N.B.4    Wines, M.5    Feig, L.A.6    Silva, A.J.7
  • 20
    • 0025028911 scopus 로고
    • Microtubule-associated-protein (MAP) kinase activated by nerve growth factor and epidermal growth factor in PC12 cells. Identity with the mitogen-activated MAP kinase of fibroblastic cells
    • Gotoh, Y., Nishida, E., Yamashita, T., Hoshi, M., Kawakami, M., and Sakai, H. (1990). Microtubule-associated-protein (MAP) kinase activated by nerve growth factor and epidermal growth factor in PC12 cells. Identity with the mitogen-activated MAP kinase of fibroblastic cells. Eur. J. Biochem. 193, 661-669.
    • (1990) Eur. J. Biochem. , vol.193 , pp. 661-669
    • Gotoh, Y.1    Nishida, E.2    Yamashita, T.3    Hoshi, M.4    Kawakami, M.5    Sakai, H.6
  • 21
    • 0023038434 scopus 로고
    • Activated N-ras gene induces neuronal differentiation of PC12 rat pheochromocytoma cells
    • Guerrero, I., Wong, H., Pellicer, A., and Burstein, D. E. (1986). Activated N-ras gene induces neuronal differentiation of PC12 rat pheochromocytoma cells. J. Cell. Physiol. 129, 71-76.
    • (1986) J. Cell. Physiol. , vol.129 , pp. 71-76
    • Guerrero, I.1    Wong, H.2    Pellicer, A.3    Burstein, D.E.4
  • 22
    • 0032577563 scopus 로고    scopus 로고
    • S. typhimurium encodes an activator of Rho GTPases that induces membrane ruffling and nuclear responses in host cells
    • Hardt, W. D., Chen, L. M., Schuebel, K. E., Bustelo, X. R., and Galan, J. E. (1998). S. typhimurium encodes an activator of Rho GTPases that induces membrane ruffling and nuclear responses in host cells. Cell 93, 815-826.
    • (1998) Cell , vol.93 , pp. 815-826
    • Hardt, W.D.1    Chen, L.M.2    Schuebel, K.E.3    Bustelo, X.R.4    Galan, J.E.5
  • 23
    • 0037308836 scopus 로고    scopus 로고
    • Ras-effector interactions: After one decade
    • Herrmann, C. (2003). Ras-effector interactions: after one decade. Curr. Opin. Struct. Biol. 33, 122-129.
    • (2003) Curr. Opin. Struct. Biol. , vol.33 , pp. 122-129
    • Herrmann, C.1
  • 24
    • 0034739850 scopus 로고    scopus 로고
    • Transgenic activation of Ras in neurons promotes hypertrophy and protects from lesion-induced degeneration
    • Heumann, R. et al. (2000). Transgenic activation of Ras in neurons promotes hypertrophy and protects from lesion-induced degeneration. J. Cell Biol. 151, 1537-1548.
    • (2000) J. Cell Biol. , vol.151 , pp. 1537-1548
    • Heumann, R.1
  • 25
    • 0032722971 scopus 로고    scopus 로고
    • CDC25(Mm)/Ras-GRF1 regulates both Ras and Rac signaling pathways
    • Innocenti, M., Zippel, R., Brambilla, R., and Sturani, E. (1999). CDC25(Mm)/Ras-GRF1 regulates both Ras and Rac signaling pathways. FEBS Lett. 460, 357-362.
    • (1999) FEBS Lett. , vol.460 , pp. 357-362
    • Innocenti, M.1    Zippel, R.2    Brambilla, R.3    Sturani, E.4
  • 26
    • 0031029870 scopus 로고    scopus 로고
    • Induction of a distinct morphology and signal transduction in TrkB/PC12 cells by nerve growth factor and brain-derived neurotrophic factor
    • Iwasaki, Y., Ishikawa, M., Okada, N., and Koizumi, S. (1997). Induction of a distinct morphology and signal transduction in TrkB/PC12 cells by nerve growth factor and brain-derived neurotrophic factor. J. Neurochem. 68, 927-934.
    • (1997) J. Neurochem. , vol.68 , pp. 927-934
    • Iwasaki, Y.1    Ishikawa, M.2    Okada, N.3    Koizumi, S.4
  • 28
    • 0031917171 scopus 로고    scopus 로고
    • Ras-GRF activates Ha-Ras, but not N-Ras or K-Ras 4B, protein in vivo
    • Jones, M. K., and Jackson, J. H. (1998). Ras-GRF activates Ha-Ras, but not N-Ras or K-Ras 4B, protein in vivo. J. Biol. Chem. 273, 1782-1787.
    • (1998) J. Biol. Chem. , vol.273 , pp. 1782-1787
    • Jones, M.K.1    Jackson, J.H.2
  • 29
    • 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., and Satoh, T. (2000a). Stimulation of Ras guanine nucleotide exchange activity of Ras-GRF1/CDC25(Mm) upon tyrosine phosphorylation by the Cdc42-regulated kinase ACK1. J. Biol. Chem. 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
  • 30
    • 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., and Satoh, T. (2000b). Induction of rac-guanine nucleotide exchange activity of Ras-GRF1/CDC25(Mm) following phosphorylation by the nonreceptor tyrosine kinase Src. J. Biol. Chem. 275, 5441-5446.
    • (2000) J. Biol. Chem. , vol.275 , pp. 5441-5446
    • Kiyono, M.1    Kaziro, Y.2    Satoh, T.3
  • 31
    • 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., and Kaziro, Y. (1999). G protein beta gamma subunit-dependent Rac-guanine nucleotide exchange activity of Ras-GRF1/CDC25(Mm). Proc. Natl. Acad. Sci. USA 96, 4826-4831.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 4826-4831
    • Kiyono, M.1    Satoh, T.2    Kaziro, Y.3
  • 34
    • 0035855710 scopus 로고    scopus 로고
    • A role for the PI-3 kinase signaling pathway in fear conditioning and synaptic plasticity in the amygdala
    • Lin, C. H., Yeh, S. H., Lin, C. H., Lu, K. T., Leu, T. H., Chang, W. C., and Gean, P. W. (2001). A role for the PI-3 kinase signaling pathway in fear conditioning and synaptic plasticity in the amygdala. Neuron 31, 841-851.
    • (2001) Neuron , vol.31 , pp. 841-851
    • Lin, C.H.1    Yeh, S.H.2    Lin, C.H.3    Lu, K.T.4    Leu, T.H.5    Chang, W.C.6    Gean, P.W.7
  • 36
    • 0030026182 scopus 로고    scopus 로고
    • Differential effects of the Rac GTPase on Purkinje cell axons and dendritic trunks and spines
    • Luo, L., Hensch, T. K., Ackerman, L., Barbel, S., Jan, L. Y., and Jan, Y. N. (1996). Differential effects of the Rac GTPase on Purkinje cell axons and dendritic trunks and spines. Nature 379, 837-840.
    • (1996) Nature , vol.379 , pp. 837-840
    • Luo, L.1    Hensch, T.K.2    Ackerman, L.3    Barbel, S.4    Jan, L.Y.5    Jan, Y.N.6
  • 38
    • 0033376412 scopus 로고    scopus 로고
    • Activity-dependent interaction of the intracellular domain of rat rrkA with intermediate filament proteins, the beta-6 proteasomal subunit, Ras-GRF1, and the p162 subunit of eIF3
    • MacDonald, J. I., Verdi, J. M., and Meakin, S. O. (1999). Activity-dependent interaction of the intracellular domain of rat rrkA with intermediate filament proteins, the beta-6 proteasomal subunit, Ras-GRF1, and the p162 subunit of eIF3. J. Mol. Neurosci. 23, 141-158.
    • (1999) J. Mol. Neurosci. , vol.23 , pp. 141-158
    • MacDonald, J.I.1    Verdi, J.M.2    Meakin, S.O.3
  • 39
    • 0035222855 scopus 로고    scopus 로고
    • The ras signaling pathway in mammary tumorigenesis and metastasis
    • Malaney, S., and Daly, R. J. (2001). The ras signaling pathway in mammary tumorigenesis and metastasis. J. Mammary Gland Biol. Neoplasia 6, 101-113.
    • (2001) J. Mammary Gland Biol. Neoplasia , vol.6 , pp. 101-113
    • Malaney, S.1    Daly, R.J.2
  • 40
    • 0034175488 scopus 로고    scopus 로고
    • Regulation of long-term potentiation by H-Ras through NMDA receptor phosphorylation
    • Manabe, T., Aiba, A., Yamada, A., Ichise, T., Sakagami, H., Kondo, H., and Katsuki, M. (2000). Regulation of long-term potentiation by H-Ras through NMDA receptor phosphorylation. J. Neurosci. 20, 2504-2511.
    • (2000) J. Neurosci. , vol.20 , pp. 2504-2511
    • Manabe, T.1    Aiba, A.2    Yamada, A.3    Ichise, T.4    Sakagami, H.5    Kondo, H.6    Katsuki, M.7
  • 42
    • 0344885558 scopus 로고    scopus 로고
    • Structural evidence for feedback activation by Ras.GTP of the Ras-specific nucleotide exchange factor SOS
    • Margarit, S. M., Sondermann, H., Hall, B. E., Nagar, B., Hoelz, A., Pirruccello, M., Bar-Sagi, D., and Kuriyan, J. (2003). Structural evidence for feedback activation by Ras.GTP of the Ras-specific nucleotide exchange factor SOS. Cell 112, 685-695.
    • (2003) Cell , vol.112 , pp. 685-695
    • Margarit, S.M.1    Sondermann, H.2    Hall, B.E.3    Nagar, B.4    Hoelz, A.5    Pirruccello, M.6    Bar-Sagi, D.7    Kuriyan, J.8
  • 43
    • 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., and Alberghina, L. (1992). Cloning by functional complementation of a mouse cDNA encoding a homologue of CDC25, a Saccharomyces cerevisiae RAS activator. EMBO J. 23, 2151-2157.
    • (1992) EMBO J. , vol.23 , 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
  • 44
    • 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. (1999). Phosphorylation of serine 916 of Ras-GRF1 contributes to the activation of exchange factor activity by muscarinic receptors. J. Biol. Chem. 274, 37379-37384.
    • (1999) J. Biol. Chem. , vol.274 , pp. 37379-37384
    • Mattingly, R.R.1
  • 45
    • 0035516589 scopus 로고    scopus 로고
    • Low concentrations of inorganic mercury inhibit Ras activation during T cell receptor-mediated signal transduction
    • Mattingly, R. R., Felczak, A., Chen, C. C., McCabe, M. J., and Rosenspire, A. J. (2001a). Low concentrations of inorganic mercury inhibit Ras activation during T cell receptor-mediated signal transduction. Toxicol. Appl. Pharmacol. 176, 162-168.
    • (2001) Toxicol. Appl. Pharmacol. , vol.176 , pp. 162-168
    • Mattingly, R.R.1    Felczak, A.2    Chen, C.C.3    McCabe, M.J.4    Rosenspire, A.J.5
  • 46
    • 29244466812 scopus 로고    scopus 로고
    • The mitogen-activated protein kinase/extracellular signal-regulated kinase kinase inhibitor PD184352 (CI-1040) selectively induces apoptosis in malignant Schwannoma cell lines
    • Mattingly, R. R., Kraniak, J. M., Dilworth, J. T., Mathieu, P., Bealmear, B., Nowak, J. E., Benjamins, J. A., Tainsky, M. A., and Reiners, J. J., Jr. (2006). The mitogen-activated protein kinase/extracellular signal-regulated kinase kinase inhibitor PD184352 (CI-1040) selectively induces apoptosis in malignant Schwannoma cell lines. J. Pharmacol. Exp. Ther. 316, 456-465.
    • (2006) J. Pharmacol. Exp. Ther. , vol.316 , pp. 456-465
    • Mattingly, R.R.1    Kraniak, J.M.2    Dilworth, J.T.3    Mathieu, P.4    Bealmear, B.5    Nowak, J.E.6    Benjamins, J.A.7    Tainsky, M.A.8    Reiners Jr., J.J.9
  • 47
    • 0029664925 scopus 로고    scopus 로고
    • Phosphorylation-dependent activation of the Ras-GRF/CDC25(Mm) exchange factor by muscarinic receptors and G-protein beta gamma subunits
    • Mattingly, R. R., and Macara, I. G. (1996). Phosphorylation-dependent activation of the Ras-GRF/CDC25(Mm) exchange factor by muscarinic receptors and G-protein beta gamma subunits. Nature 382, 268-272.
    • (1996) Nature , vol.382 , pp. 268-272
    • Mattingly, R.R.1    Macara, I.G.2
  • 48
    • 0034970001 scopus 로고    scopus 로고
    • Down-regulation of growth factor-stimulated MAP kinase signaling in cytotoxic drug-resistant human neuroblastoma cells
    • Mattingly, R. R., Milstein, M. L., and Mirkin, B. L. (2001b). Down-regulation of growth factor-stimulated MAP kinase signaling in cytotoxic drug-resistant human neuroblastoma cells. Cell Signal. 23, 499-505.
    • (2001) Cell Signal. , vol.23 , pp. 499-505
    • Mattingly, R.R.1    Milstein, M.L.2    Mirkin, B.L.3
  • 49
    • 0033057582 scopus 로고    scopus 로고
    • Activation of the Ras-GRF/CDC25(Mm) exchange factor by lysophosphatidic acid
    • Mattingly, R. R., Saini, V., and Macara, I. G. (1999). Activation of the Ras-GRF/CDC25(Mm) exchange factor by lysophosphatidic acid. Cell Signal. 11, 603-610.
    • (1999) Cell Signal. , vol.11 , pp. 603-610
    • Mattingly, R.R.1    Saini, V.2    Macara, I.G.3
  • 50
    • 0028109685 scopus 로고
    • Muscarinic receptors transform Nih 3t3 cells through a Ras-dependent signaling pathway inhibited by the Ras-Gtpase-activating protein Sh3 domain
    • Mattingly, R. R., Sorisky, A., Brann, M. R., and Macara, I. G. (1994). Muscarinic receptors transform Nih 3t3 cells through a Ras-dependent signaling pathway inhibited by the Ras-Gtpase-activating protein Sh3 domain. Mol. Cell. Biol. 14, 7943-7952.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 7943-7952
    • Mattingly, R.R.1    Sorisky, A.2    Brann, M.R.3    Macara, I.G.4
  • 51
    • 23244467708 scopus 로고    scopus 로고
    • Active p21-activated kinase 1 rescues MCF10A breast epithelial cells from undergoing anoikis
    • Menard, R. E., Jovanovski, A. P., and Mattingly, R. R. (2005). Active p21-activated kinase 1 rescues MCF10A breast epithelial cells from undergoing anoikis. Neoplasia 7, 638-645.
    • (2005) Neoplasia , vol.7 , pp. 638-645
    • Menard, R.E.1    Jovanovski, A.P.2    Mattingly, R.R.3
  • 52
    • 0142027033 scopus 로고    scopus 로고
    • Cell surface receptors activate p21-activated kinase 1 via multiple Ras and PI3-kinase-dependent pathways
    • Menard, R. E., and Mattingly, R. R. (2003). Cell surface receptors activate p21-activated kinase 1 via multiple Ras and PI3-kinase-dependent pathways. Cell Signal. 15, 1099-1109.
    • (2003) Cell Signal. , vol.15 , pp. 1099-1109
    • Menard, R.E.1    Mattingly, R.R.2
  • 53
    • 0032559211 scopus 로고    scopus 로고
    • Coupling of Ras and Rac guanosine triphosphatases through the Ras exchanger Sos
    • Nimnual, A. S., Yatsula, B. A., and Bar-Sagi, D. (1998). Coupling of Ras and Rac guanosine triphosphatases through the Ras exchanger Sos. Science 279, 560-563.
    • (1998) Science , vol.279 , pp. 560-563
    • Nimnual, A.S.1    Yatsula, B.A.2    Bar-Sagi, D.3
  • 54
    • 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., and Levy, F. O. (2005). Endogenous expression and protein kinase A-dependent phosphorylation of the guanine nucleotide exchange factor Ras-GRF1 in human embryonic kidney 293 cells. FEBS J. 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
  • 55
    • 0037184086 scopus 로고    scopus 로고
    • Nerve growth factor signals through TrkA, phosphatidylinositol 3-kinase, and Rac1 to inactivate RhoA during the initiation of neuronal differentiation of PC12 cells
    • Nusser, N., Gosmanova, E., Zheng, Y., and Tigyi, G. (2002). Nerve growth factor signals through TrkA, phosphatidylinositol 3-kinase, and Rac1 to inactivate RhoA during the initiation of neuronal differentiation of PC12 cells. J. Biol. Chem. 277, 35840-35846.
    • (2002) J. Biol. Chem. , vol.277 , pp. 35840-35846
    • Nusser, N.1    Gosmanova, E.2    Zheng, Y.3    Tigyi, G.4
  • 56
    • 0035139220 scopus 로고    scopus 로고
    • The neuronal Rho-GEF Kalirin-7 interacts with PDZ domain-containing proteins and regulates dendritic morphogenesis
    • Penzes, P., Johnson, R. C., Sattler, R., Zhang, X., Huganir, R. L., Kambampati, V., Mains, R. E., and Eipper, B. A. (2001). The neuronal Rho-GEF Kalirin-7 interacts with PDZ domain-containing proteins and regulates dendritic morphogenesis. Neuron 29, 229-242.
    • (2001) Neuron , vol.29 , pp. 229-242
    • Penzes, P.1    Johnson, R.C.2    Sattler, R.3    Zhang, X.4    Huganir, R.L.5    Kambampati, V.6    Mains, R.E.7    Eipper, B.A.8
  • 57
    • 0032751298 scopus 로고    scopus 로고
    • Raf-like Ras/Rap-binding domains in RGS12- and still-life-like signalling proteins
    • Ponting, C. P. (1999). Raf-like Ras/Rap-binding domains in RGS12- and still-life-like signalling proteins. J. Mol. Med. 77, 695-698.
    • (1999) J. Mol. Med. , vol.77 , pp. 695-698
    • Ponting, C.P.1
  • 58
    • 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., and Castro, A. F. (2002). A growing family of guanine nucleotide exchange factors is responsible for activation of Ras-family GTPases. Prog Nucleic Acid. Res. Mol. Biol. 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
  • 60
    • 0030921287 scopus 로고    scopus 로고
    • The MEKK-JNK pathway is stimulated by alpha1-adrenergic receptor and ras activation and is associated with in vitro and in vivo cardiac hypertrophy
    • Ramirez, M. T., Sah, V. P., Zhao, X. L., Hunter, J. J., Chien, K. R., and Brown, J. H. (1997). The MEKK-JNK pathway is stimulated by alpha1-adrenergic receptor and ras activation and is associated with in vitro and in vivo cardiac hypertrophy. J. Biol. Chem. 272, 14057-14061.
    • (1997) J. Biol. Chem. , vol.272 , pp. 14057-14061
    • Ramirez, M.T.1    Sah, V.P.2    Zhao, X.L.3    Hunter, J.J.4    Chien, K.R.5    Brown, J.H.6
  • 61
    • 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., and Meakin, S. O. (2005). 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. 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
  • 63
    • 0033988255 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase, Cdc42, and Rac1 act downstream of Ras in integrin-dependent neurite outgrowth in N1E-115 neuroblastoma cells
    • Sarner, S., Kozma, R., Ahmed, S., and Lim, L. (2000). Phosphatidylinositol 3-kinase, Cdc42, and Rac1 act downstream of Ras in integrin-dependent neurite outgrowth in N1E-115 neuroblastoma cells. Mol. Cell. Biol. 20, 158-172.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 158-172
    • Sarner, S.1    Kozma, R.2    Ahmed, S.3    Lim, L.4
  • 64
    • 13944278759 scopus 로고    scopus 로고
    • Calmodulin-dependent kinase kinase/calmodulin kinase 1 activity gates extracellular-regulated kinase-dependent long-term potentiation
    • Schmitt, J. M., Guire, E. S., Saneyoshi, T., and Soderling, T. R. (2005). Calmodulin-dependent kinase kinase/calmodulin kinase 1 activity gates extracellular-regulated kinase-dependent long-term potentiation. J. Neurosci. 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
  • 65
    • 0037174634 scopus 로고    scopus 로고
    • Postsynaptic signaling and plasticity mechanisms
    • Sheng, M., and Kim, M. J. (2002). Postsynaptic signaling and plasticity mechanisms. Science 298, 776-780.
    • (2002) Science , vol.298 , pp. 776-780
    • Sheng, M.1    Kim, M.J.2
  • 66
    • 0026659515 scopus 로고
    • Molecular cloning of cDNAs encoding a guanine-nucleotide-releasing factor for Ras p21
    • Shou, C., Farnsworth, C. L., Neel, B. G., and Feig, L. A. (1992). Molecular cloning of cDNAs encoding a guanine-nucleotide-releasing factor for Ras p21. Nature 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
  • 67
    • 0029017628 scopus 로고
    • Differential response of the Ras exchange factor, Ras-GRF to tyrosine kinase and G protein mediated signals
    • Shou, C., Wurmser, A., Suen, K. L., Barbacid, M., Feig, L. A., and Ling, K. (1995). Differential response of the Ras exchange factor, Ras-GRF to tyrosine kinase and G protein mediated signals. Oncogene 10, 1887-1893.
    • (1995) Oncogene , vol.10 , pp. 1887-1893
    • Shou, C.1    Wurmser, A.2    Suen, K.L.3    Barbacid, M.4    Feig, L.A.5    Ling, K.6
  • 68
    • 0037453716 scopus 로고    scopus 로고
    • Modulation of Rho GTPase signaling regulates a switch between adipogenesis and myogenesis
    • Sordella, R., Jiang, W., Chen, G. C, Curto, M., and Settleman, J. (2003). Modulation of Rho GTPase signaling regulates a switch between adipogenesis and myogenesis. Cell 113, 147-158.
    • (2003) Cell , vol.113 , pp. 147-158
    • Sordella, R.1    Jiang, W.2    Chen, G.C.3    Curto, M.4    Settleman, J.5
  • 69
    • 0035312395 scopus 로고    scopus 로고
    • GEFs: Master regulators of G-protein activation
    • Sprang, S. (2001). GEFs: master regulators of G-protein activation. Trends Biochem. Sci. 26, 266-267.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 266-267
    • Sprang, S.1
  • 72
    • 0020404981 scopus 로고
    • Activation of the T24 bladder carcinoma transforming gene is linked to a single amino acid change
    • Taparowsky, E., Suard, Y., Fasano, O., Shimizu, K., Goldfarb, M., and Wigler, M. (1982). Activation of the T24 bladder carcinoma transforming gene is linked to a single amino acid change. Nature 300, 762-765.
    • (1982) Nature , vol.300 , pp. 762-765
    • Taparowsky, E.1    Suard, Y.2    Fasano, O.3    Shimizu, K.4    Goldfarb, M.5    Wigler, M.6
  • 73
    • 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., and Feig, L. A. (2004). Developmentally regulated role for Ras-GRFs in coupling NMDA glutamate receptors to Ras, Erk and CREB. EMBO J. 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
  • 74
    • 13844253719 scopus 로고    scopus 로고
    • The Rac1-GEF Tiam1 couples the NMDA receptor to the activity-dependent development of dendritic arbors and spines
    • Tolias, K. F., Bikoff, J. B., Burette, A., Paradis, S., Harrar, D., Tavazoie, S., Weinberg, R. J., and Greenberg, M. E. (2005). The Rac1-GEF Tiam1 couples the NMDA receptor to the activity-dependent development of dendritic arbors and spines. Neuron 45, 525-538.
    • (2005) Neuron , vol.45 , pp. 525-538
    • Tolias, K.F.1    Bikoff, J.B.2    Burette, A.3    Paradis, S.4    Harrar, D.5    Tavazoie, S.6    Weinberg, R.J.7    Greenberg, M.E.8
  • 75
    • 0035681050 scopus 로고    scopus 로고
    • Involvement of CDC25Mm/Ras-GRF1-dependent signaling in the control of neuronal excitability
    • Tonini, R. et al. (2001). Involvement of CDC25Mm/Ras-GRF1-dependent signaling in the control of neuronal excitability. Mol. Cell Neurosci. 18, 691-701.
    • (2001) Mol. Cell Neurosci. , vol.18 , pp. 691-701
    • Tonini, R.1
  • 76
    • 0141726829 scopus 로고    scopus 로고
    • The concerted signaling of ERK1/2 and JNKs is essential for PC12 cell neuritogenesis and converges at the level of target proteins
    • Waetzig, V., and Herdegen, T. (2003). The concerted signaling of ERK1/2 and JNKs is essential for PC12 cell neuritogenesis and converges at the level of target proteins. Mol. Cell Neurosci. 24, 238-249.
    • (2003) Mol. Cell Neurosci. , vol.24 , pp. 238-249
    • Waetzig, V.1    Herdegen, T.2
  • 77
    • 3042725682 scopus 로고    scopus 로고
    • Molecular genetics of human cognition
    • Weeber, E. J., Levenson, J. M., and Sweatt, J. D. (2002). Molecular genetics of human cognition. Mol. Interv. 2, 376-392, 339.
    • (2002) Mol. Interv. , vol.2 , pp. 376-392
    • Weeber, E.J.1    Levenson, J.M.2    Sweatt, J.D.3
  • 78
    • 0028564740 scopus 로고
    • Cloning and analysis of human cDNAs encoding a 140-kDa brain guanine nucleotide-exchange factor, Cdc25GEF, which regulates the function of Ras
    • Wei, W., Das, B., Park, W., and Broek, D. (1994). Cloning and analysis of human cDNAs encoding a 140-kDa brain guanine nucleotide-exchange factor, Cdc25GEF, which regulates the function of Ras. Gene 252, 279-284.
    • (1994) Gene , vol.252 , pp. 279-284
    • Wei, W.1    Das, B.2    Park, W.3    Broek, D.4
  • 79
    • 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., and Mattingly, R. R. (2003). Phosphorylation of the Ras-GRF1 Exchange Factor at Ser916/898 reveals activation of Ras signaling in the cerebral cortex. J. Biol. Chem. 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
  • 80
    • 0035805586 scopus 로고    scopus 로고
    • Differential responses to nerve growth factor and epidermal growth factor in neurite outgrowth of PC12 cells are determined by Rac1 activation systems
    • Yasui, H., Katoh, H., Yamaguchi, Y., Aoki, J., Fujita, H., Mori, K., and Negishi, M. (2001). Differential responses to nerve growth factor and epidermal growth factor in neurite outgrowth of PC12 cells are determined by Rac1 activation systems. J. Biol. Chem. 276, 15298-15305.
    • (2001) J. Biol. Chem. , vol.276 , pp. 15298-15305
    • Yasui, H.1    Katoh, H.2    Yamaguchi, Y.3    Aoki, J.4    Fujita, H.5    Mori, K.6    Negishi, M.7
  • 81
    • 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., and Martegani, E. (1996). The brain specific Ras exchange factor CDC25 Mm: modulation of its activity through Gi-protein-mediated signals. Oncogene 12, 2697-2703.
    • (1996) Oncogene , vol.12 , pp. 2697-2703
    • Zippel, R.1    Orecchia, S.2    Sturani, E.3    Martegani, E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.