메뉴 건너뛰기




Volumn 17, Issue 3, 2006, Pages 1204-1217

Deregulation of HEF1 impairs M-phase progression by disrupting the RhoA activation cycle

Author keywords

[No Author keywords available]

Indexed keywords

CELLULAR APOPTOSIS SUSCEPTIBILITY PROTEIN; PROTEIN ECT2; PROTEIN HEF1; RHOA GUANINE NUCLEOTIDE BINDING PROTEIN; SMALL INTERFERING RNA; UNCLASSIFIED DRUG;

EID: 33644868709     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E05-03-0237     Document Type: Article
Times cited : (50)

References (73)
  • 1
    • 0029766101 scopus 로고    scopus 로고
    • Coordinate activation of c-Src by SH3- and SH2-binding sites on a novel, p130Cas-related protein
    • Alexandropoulos, K., and Baltimore, D. (1996). Coordinate activation of c-Src by SH3- and SH2-binding sites on a novel, p130Cas-related protein, Sin. Genes Dev. 10, 1341-1355.
    • (1996) Sin. Genes Dev. , vol.10 , pp. 1341-1355
    • Alexandropoulos, K.1    Baltimore, D.2
  • 2
    • 0034116930 scopus 로고    scopus 로고
    • Disruption of the murine calpain small subunit gene, Capn 4, calpain is essential for embryonic development but not for cell growth and division
    • Arthur, J. S., Eke, J. S., Hegadorn, C., Williams, K., and Greer, P. A. (2000). Disruption of the murine calpain small subunit gene, Capn 4, calpain is essential for embryonic development but not for cell growth and division. Mol. Cell. Biol. 20, 4474-4481.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 4474-4481
    • Arthur, J.S.1    Eke, J.S.2    Hegadorn, C.3    Williams, K.4    Greer, P.A.5
  • 3
    • 0035158377 scopus 로고    scopus 로고
    • RhoA inactivation by p190RhoGAP regulates cell spreading and migration by promoting membrane protrusion and polarity
    • Arthur, W. T., and Burridge, K. (2001). RhoA inactivation by p190RhoGAP regulates cell spreading and migration by promoting membrane protrusion and polarity. Mol. Biol. Cell 12, 2711-2720.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 2711-2720
    • Arthur, W.T.1    Burridge, K.2
  • 4
    • 0036400641 scopus 로고    scopus 로고
    • Regulation of Rho family GTPases by cell-cell and cell-matrix adhesion
    • Arthur, W. T., Noren, N. K., and Burridge, K. (2002). Regulation of Rho family GTPases by cell-cell and cell-matrix adhesion. Biol. Res. 35, 239-246.
    • (2002) Biol. Res. , vol.35 , pp. 239-246
    • Arthur, W.T.1    Noren, N.K.2    Burridge, K.3
  • 5
    • 28844479472 scopus 로고    scopus 로고
    • The Cas family docking protein, HEF1, promotes the formation of neurite-like membrane extensions
    • Bargon, S. D., Gunning, P. W., and O'Neill, G. M. (2005). The Cas family docking protein, HEF1, promotes the formation of neurite-like membrane extensions. Biochim. Biophys. Acta 1746, 143-154.
    • (2005) Biochim. Biophys. Acta , vol.1746 , pp. 143-154
    • Bargon, S.D.1    Gunning, P.W.2    O'Neill, G.M.3
  • 6
    • 0019833279 scopus 로고
    • Multinudeation and inhibition of cytokinesis in suspended cells: Reversal upon reattachment to a substrate
    • Ben-Ze'ev, A., and Raz, A. (1981). Multinudeation and inhibition of cytokinesis in suspended cells: reversal upon reattachment to a substrate. Cell 26, 107-115.
    • (1981) Cell , vol.26 , pp. 107-115
    • Ben-Ze'ev, A.1    Raz, A.2
  • 7
    • 0031713433 scopus 로고    scopus 로고
    • Extracellular matrix signaling, integration of form and function in normal and malignant cells
    • Boudreau, N., and Bissell, M. J. (1998). Extracellular matrix signaling, integration of form and function in normal and malignant cells. Curr. Opin. Cell Biol. 10, 640-646.
    • (1998) Curr. Opin. Cell Biol. , vol.10 , pp. 640-646
    • Boudreau, N.1    Bissell, M.J.2
  • 8
    • 0035474419 scopus 로고    scopus 로고
    • Functions of the adapter protein Cas: Signal convergence and the determination of cellular responses
    • Bouton, A. H., Riggins, R. B., and Bruce-Staskal, P. J. (2001). Functions of the adapter protein Cas: signal convergence and the determination of cellular responses. Oncogene 20, 6448-6458.
    • (2001) Oncogene , vol.20 , pp. 6448-6458
    • Bouton, A.H.1    Riggins, R.B.2    Bruce-Staskal, P.J.3
  • 9
    • 0031013074 scopus 로고    scopus 로고
    • Traction forces of cytokinesis measured with optically modified elastic substrata
    • Burton, K., and Taylor, D. L. (1997). Traction forces of cytokinesis measured with optically modified elastic substrata. Nature 385, 450-454.
    • (1997) Nature , vol.385 , pp. 450-454
    • Burton, K.1    Taylor, D.L.2
  • 10
    • 0037072731 scopus 로고    scopus 로고
    • Roles of Rho-associated kinase and myosin light chain kinase in morphological and migratory defects of focal adhesion kinase-null cells
    • Chen, B. H., Tzen, J. T., Bresnick, A. R., and Chen, H. C. (2002). Roles of Rho-associated kinase and myosin light chain kinase in morphological and migratory defects of focal adhesion kinase-null cells. J. Biol. Chem. 277, 33857-33863.
    • (2002) J. Biol. Chem. , vol.277 , pp. 33857-33863
    • Chen, B.H.1    Tzen, J.T.2    Bresnick, A.R.3    Chen, H.C.4
  • 11
    • 15844402150 scopus 로고    scopus 로고
    • Melatonin inhibits DNA synthesis in MCF-7 human breast cancer cells in vitro
    • Cos, S., Fernandez, F., and Sanchez-Barcelo, E. J. (1996). Melatonin inhibits DNA synthesis in MCF-7 human breast cancer cells in vitro. Life Sci. 58, 2447-2453.
    • (1996) Life Sci. , vol.58 , pp. 2447-2453
    • Cos, S.1    Fernandez, F.2    Sanchez-Barcelo, E.J.3
  • 12
    • 0037164867 scopus 로고    scopus 로고
    • The fibronectin-binding integrins alpha5beta1 and alphavbeta3 differentially modulate RhoA-GTP loading, organization of cell matrix adhesions, and fibronectin fibrillogenesis
    • Danen, E. H., Sonneveld, P., Brakebusch, C., Fassler, R., and Sonnenberg, A. (2002). The fibronectin-binding integrins alpha5beta1 and alphavbeta3 differentially modulate RhoA-GTP loading, organization of cell matrix adhesions, and fibronectin fibrillogenesis. J. Cell Biol. 159, 1071-1086.
    • (2002) J. Cell Biol. , vol.159 , pp. 1071-1086
    • Danen, E.H.1    Sonneveld, P.2    Brakebusch, C.3    Fassler, R.4    Sonnenberg, A.5
  • 13
    • 0037347196 scopus 로고    scopus 로고
    • Centrosome separation and central spindle assembly act in redundant pathways that regulate microtubule density and trigger cleavage furrow formation
    • Dechant, R., and Glotzer, M. (2003). Centrosome separation and central spindle assembly act in redundant pathways that regulate microtubule density and trigger cleavage furrow formation. Dev. Cell 4, 333-344.
    • (2003) Dev. Cell , vol.4 , pp. 333-344
    • Dechant, R.1    Glotzer, M.2
  • 14
    • 2942661328 scopus 로고    scopus 로고
    • Suppression of p160ROCK bypasses cell cycle arrest after Aurora-A/STK15 depletion
    • Du, J., and Hannon, G. J. (2004). Suppression of p160ROCK bypasses cell cycle arrest after Aurora-A/STK15 depletion. Proc. Natl. Acad. Sci. USA 101, 8975-8980.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 8975-8980
    • Du, J.1    Hannon, G.J.2
  • 15
    • 0036153173 scopus 로고    scopus 로고
    • Dissection of HEF1-dependent functions in motility and transcriptional regulation
    • Fashena, S. J., Einarson, M. B., O'Neill, G. M., Patriotis, C. P., and Golemis, E. A. (2002). Dissection of HEF1-dependent functions in motility and transcriptional regulation. J. Cell Sci. 115, 99-111.
    • (2002) J. Cell Sci. , vol.115 , pp. 99-111
    • Fashena, S.J.1    Einarson, M.B.2    O'Neill, G.M.3    Patriotis, C.P.4    Golemis, E.A.5
  • 16
    • 0029892628 scopus 로고    scopus 로고
    • Rho stimulates tyrosine phosphorylation of focal adhesion kinase, p130 and paxillin
    • Flinn, H. M., and Ridley, A. J. (1996). Rho stimulates tyrosine phosphorylation of focal adhesion kinase, p130 and paxillin. J. Cell Sci. 109, 1133-1141.
    • (1996) J. Cell Sci. , vol.109 , pp. 1133-1141
    • Flinn, H.M.1    Ridley, A.J.2
  • 17
    • 0035447707 scopus 로고    scopus 로고
    • Cell-cycledependent association of protein phosphatase 1 and focal adhesion kinase
    • Fresu, M., Bianchi, M., Parsons, J. T., and Villa-Moruzzi, E. (2001). Cell-cycledependent association of protein phosphatase 1 and focal adhesion kinase. Biochem. J. 358, 407-414.
    • (2001) Biochem. J. , vol.358 , pp. 407-414
    • Fresu, M.1    Bianchi, M.2    Parsons, J.T.3    Villa-Moruzzi, E.4
  • 18
    • 0028057613 scopus 로고
    • Disruption of epithelial cell-matrix interactions induces apoptosis
    • Frisch, S. M., and Francis, H. (1994). Disruption of epithelial cell-matrix interactions induces apoptosis. J. Cell Biol. 124, 619-626.
    • (1994) J. Cell Biol. , vol.124 , pp. 619-626
    • Frisch, S.M.1    Francis, H.2
  • 19
    • 0032300175 scopus 로고    scopus 로고
    • Cell cycle-dependent proteolysis in plants. Identification of the destruction box pathway and metaphase arrest produced by the proteasome inhibitor mg132
    • Genschik, P., Criqui, M. C., Parmentier, Y., Derevier, A., and Fleck, J. (1998). Cell cycle-dependent proteolysis in plants. Identification Of the destruction box pathway and metaphase arrest produced by the proteasome inhibitor mg132. Plant Cell 10, 2063-2076.
    • (1998) Plant Cell , vol.10 , pp. 2063-2076
    • Genschik, P.1    Criqui, M.C.2    Parmentier, Y.3    Derevier, A.4    Fleck, J.5
  • 20
    • 0032550181 scopus 로고    scopus 로고
    • A role for Dictyostelium racE in cortical tension and cleavage furrow progression
    • Gerald, N., Dai, J., Ting-Beall, H. P., and De Lozanne, A. (1998). A role for Dictyostelium racE in cortical tension and cleavage furrow progression. J. Cell Biol. 141, 483-492.
    • (1998) J. Cell Biol. , vol.141 , pp. 483-492
    • Gerald, N.1    Dai, J.2    Ting-Beall, H.P.3    De Lozanne, A.4
  • 21
  • 22
    • 18544412767 scopus 로고    scopus 로고
    • Zyxin, a regulator of actin filament assembly, targets the mitotic apparatus by interacting with h-warts/LATS1 tumor suppressor
    • Hirota, T., Morisaki, T., Nishiyama, Y., Marumoto, T., Tada, K., Hara, T., Masuko, N., Inagaki, M., Hatakeyama, K., and Saya, H. (2000). Zyxin, a regulator of actin filament assembly, targets the mitotic apparatus by interacting with h-warts/LATS1 tumor suppressor. J. Cell Biol. 149, 1073-1086.
    • (2000) J. Cell Biol. , vol.149 , pp. 1073-1086
    • Hirota, T.1    Morisaki, T.2    Nishiyama, Y.3    Marumoto, T.4    Tada, K.5    Hara, T.6    Masuko, N.7    Inagaki, M.8    Hatakeyama, K.9    Saya, H.10
  • 23
    • 0029083385 scopus 로고
    • Suppression of v-Src transformation in primary rat embryo fibroblasts
    • Inoue, H., Tavoloni, N., and Hanafusa, H. (1995). Suppression of v-Src transformation in primary rat embryo fibroblasts. Oncogene 11, 231-238.
    • (1995) Oncogene , vol.11 , pp. 231-238
    • Inoue, H.1    Tavoloni, N.2    Hanafusa, H.3
  • 24
    • 0029562687 scopus 로고
    • Molecular cloning of a cDNA encoding a phosphoprotein, Efs, which contains a Src homology 3 domain and associates with Fyn
    • Ishino, M., Ohba, T., Sasaki, H., and Sasaki, T. (1995). Molecular cloning of a cDNA encoding a phosphoprotein, Efs, which contains a Src homology 3 domain and associates with Fyn. Oncogene 11, 2331-2338.
    • (1995) Oncogene , vol.11 , pp. 2331-2338
    • Ishino, M.1    Ohba, T.2    Sasaki, H.3    Sasaki, T.4
  • 26
    • 14044263688 scopus 로고    scopus 로고
    • The tandem BRCT domains of Ect2 are required for both negative and positive regulation of Ect2 in cytokinesis
    • Kim, J. E., Billadeau, D. D., and Chen, J. (2005). The tandem BRCT domains of Ect2 are required for both negative and positive regulation of Ect2 in cytokinesis. J. Biol. Chem. 280, 5733-5739.
    • (2005) J. Biol. Chem. , vol.280 , pp. 5733-5739
    • Kim, J.E.1    Billadeau, D.D.2    Chen, J.3
  • 27
    • 0034625353 scopus 로고    scopus 로고
    • Accumulation of GTP-bound RhoA during cytokinesis and a critical role of ECT2 in this accumulation
    • Kimura, K., Tsuji, T., Takada, Y., Miki, T., and Narumiya, S. (2000). Accumulation of GTP-bound RhoA during cytokinesis and a critical role of ECT2 in this accumulation. J. Biol. Chem. 275, 17233-17236.
    • (2000) J. Biol. Chem. , vol.275 , pp. 17233-17236
    • Kimura, K.1    Tsuji, T.2    Takada, Y.3    Miki, T.4    Narumiya, S.5
  • 28
    • 0030045346 scopus 로고    scopus 로고
    • Cell migration: A physically integrated molecular process
    • Lauffenburger, D. A., and Horwitz, A. F. (1996). Cell migration: a physically integrated molecular process. Cell 84, 359-369.
    • (1996) Cell , vol.84 , pp. 359-369
    • Lauffenburger, D.A.1    Horwitz, A.F.2
  • 29
    • 0029891787 scopus 로고    scopus 로고
    • Human Enhancer of Filamentation 1 (HEF1), a novel p130Cas-like docking protein, associates with FAK, and induces pseudohyphal growth in yeast
    • Law, S. F., Estojak, J., Wang, B., Mysliwiec, T., Kruh, G. D., and Golemis, E. A. (1996). Human Enhancer of Filamentation 1 (HEF1), a novel p130Cas-like docking protein, associates with FAK, and induces pseudohyphal growth in yeast. Mol. Cell Biol. 16, 3327-3337.
    • (1996) Mol. Cell Biol. , vol.16 , pp. 3327-3337
    • Law, S.F.1    Estojak, J.2    Wang, B.3    Mysliwiec, T.4    Kruh, G.D.5    Golemis, E.A.6
  • 30
    • 0033934340 scopus 로고    scopus 로고
    • The docking protein HEF1 is an apoptotic mediator at focal adhesion sites
    • Law, S. F., O'Neill, G. M., Fashena, S. J., Einarson, M. B., and Golemis, E. A. (2000). The docking protein HEF1 is an apoptotic mediator at focal adhesion sites. Mol. Cell Biol. 20, 5184-5195.
    • (2000) Mol. Cell Biol. , vol.20 , pp. 5184-5195
    • Law, S.F.1    O'Neill, G.M.2    Fashena, S.J.3    Einarson, M.B.4    Golemis, E.A.5
  • 31
    • 0031813880 scopus 로고    scopus 로고
    • Cell-cycle regulated processing of HEF1 to multiple protein forms differentially targeted to multiple compartments
    • Law, S. F., Zhang, Y.-Z., Klein-Szanto, A., and Golemis, E. A. (1998). Cell-cycle regulated processing of HEF1 to multiple protein forms differentially targeted to multiple compartments. Mol. Cell. Biol. 18, 3540-3551.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 3540-3551
    • Law, S.F.1    Zhang, Y.-Z.2    Klein-Szanto, A.3    Golemis, E.A.4
  • 32
    • 3242702211 scopus 로고    scopus 로고
    • Nucleotide exchange factor ECT2 interacts with the polarity protein complex Par6/Par3/protein kinase Czeta (PKCzeta) and regulates PKCzeta activity
    • Liu, X. F., Ishida, H., Raziuddin, R., and Miki, T. (2004). Nucleotide exchange factor ECT2 interacts with the polarity protein complex Par6/Par3/protein kinase Czeta (PKCzeta) and regulates PKCzeta activity. Mol. Cell. Biol. 24, 6665-6675.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 6665-6675
    • Liu, X.F.1    Ishida, H.2    Raziuddin, R.3    Miki, T.4
  • 33
    • 0035176458 scopus 로고    scopus 로고
    • Serine phosphorylation of focal adhesion kinase in interphase and mitosis: A possible role in modulating binding to p130(Cas)
    • Ma, A., Richardson, A., Schaefer, E. M., and Parsons, J. T. (2001). Serine phosphorylation of focal adhesion kinase in interphase and mitosis: a possible role in modulating binding to p130(Cas). Mol. Biol. Cell 12, 1-12.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 1-12
    • Ma, A.1    Richardson, A.2    Schaefer, E.M.3    Parsons, J.T.4
  • 34
    • 0037455574 scopus 로고    scopus 로고
    • RhoA is required for cortical retraction and rigidity during mitotic cell rounding
    • Maddox, A. S., and Burridge, K. (2003). RhoA is required for cortical retraction and rigidity during mitotic cell rounding. J. Cell Biol. 160, 255-265.
    • (2003) J. Cell Biol. , vol.160 , pp. 255-265
    • Maddox, A.S.1    Burridge, K.2
  • 35
    • 0038298941 scopus 로고    scopus 로고
    • Closing the GAP: A role for a RhoA GAP in cytokinesis
    • Maddox, A. S., and Oegema, K. (2003). Closing the GAP: a role for a RhoA GAP in cytokinesis. Mol. Cell 11, 846-848.
    • (2003) Mol. Cell , vol.11 , pp. 846-848
    • Maddox, A.S.1    Oegema, K.2
  • 38
    • 0035985148 scopus 로고    scopus 로고
    • Kinesin-like protein CHO1 is required for the formation of midbody matrix and the completion of cytokinesis in mammalian cells
    • Matuliene, J., and Kuriyama, R. (2002). Kinesin-like protein CHO1 is required for the formation of midbody matrix and the completion of cytokinesis in mammalian cells. Mol. Biol. Cell 13, 1832-1845.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 1832-1845
    • Matuliene, J.1    Kuriyama, R.2
  • 39
    • 0022967956 scopus 로고
    • Arrangement of actin filaments and myosin-like filaments in the contractile ring and of actin-like filaments in the mitotic spindle of dividing HeLa cells
    • Maupin, P., and Pollard, T. D. (1986). Arrangement of actin filaments and myosin-like filaments in the contractile ring and of actin-like filaments in the mitotic spindle of dividing HeLa cells. J. Ultrastruct. Mol. Struct. Res. 94, 92-103.
    • (1986) J. Ultrastruct. Mol. Struct. Res. , vol.94 , pp. 92-103
    • Maupin, P.1    Pollard, T.D.2
  • 40
    • 0037387766 scopus 로고    scopus 로고
    • Phosphorylation by aurora B converts MgcRac-GAP to a RhoGAP during cytokinesis
    • Minoshima, Y., et al. (2003). Phosphorylation by Aurora B Converts MgcRac-GAP to a RhoGAP during Cytokinesis. Dev. Cell 4, 549-560.
    • (2003) Dev. Cell , vol.4 , pp. 549-560
    • Minoshima, Y.1
  • 41
    • 0037092522 scopus 로고    scopus 로고
    • Genetic and morphological evidence for two parallel pathways of cell-cycle-coupled cytokinesis in Dictyostelium
    • Nagasaki, A., De Hostos, E. L., and Uyeda, T. Q. (2002). Genetic and morphological evidence for two parallel pathways of cell-cycle-coupled cytokinesis in Dictyostelium. J. Cell Sci. 115, 2241-2251.
    • (2002) J. Cell Sci. , vol.115 , pp. 2241-2251
    • Nagasaki, A.1    De Hostos, E.L.2    Uyeda, T.Q.3
  • 42
    • 0029945648 scopus 로고    scopus 로고
    • Direct binding of the C-terminal region of p130-Cas to SH2 and SH3 domains of Src kinase
    • Nakamoto, T., Sakai, R., Ozawa, K., Yazaki, Y., and Hirai, H. (1996). Direct binding of the C-terminal region of p130-Cas to SH2 and SH3 domains of Src kinase. J. Biol. Chem. 271, 8959-8965.
    • (1996) J. Biol. Chem. , vol.271 , pp. 8959-8965
    • Nakamoto, T.1    Sakai, R.2    Ozawa, K.3    Yazaki, Y.4    Hirai, H.5
  • 43
    • 0035735822 scopus 로고    scopus 로고
    • The pebble GTP exchange factor and the control of cytokinesis
    • O'Keefe, L., Somers, W. G., Harley, A., and Saint, R. (2001). The pebble GTP exchange factor and the control of cytokinesis. Cell Struct. Funct. 26, 619-626.
    • (2001) Cell Struct. Funct. , vol.26 , pp. 619-626
    • O'Keefe, L.1    Somers, W.G.2    Harley, A.3    Saint, R.4
  • 44
    • 0034160011 scopus 로고    scopus 로고
    • Integrin signaling: A new Cas(t) of characters enters the stage
    • O'Neill, G. M., Fashena, S. J., and Golemis, E. A. (2000). Integrin signaling: a new Cas(t) of characters enters the stage. Trends Cell Biol. 10, 111-119.
    • (2000) Trends Cell Biol. , vol.10 , pp. 111-119
    • O'Neill, G.M.1    Fashena, S.J.2    Golemis, E.A.3
  • 45
    • 0034959232 scopus 로고    scopus 로고
    • Proteolysis of the docking protein HEF1 and implications for focal adhesion dynamics
    • O'Neill, G. M., and Golemis, E. A. (2001). Proteolysis of the docking protein HEF1 and implications for focal adhesion dynamics. Mol. Cell. Biol. 21, 5094-5108.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 5094-5108
    • O'Neill, G.M.1    Golemis, E.A.2
  • 46
    • 0018742870 scopus 로고
    • Fibronectin mediates cytokinesis and growth of rat follicular cells in serum-free medium
    • Orly, J., and Sato, G. (1979). Fibronectin mediates cytokinesis and growth of rat follicular cells in serum-free medium. Cell 17, 295-305.
    • (1979) Cell , vol.17 , pp. 295-305
    • Orly, J.1    Sato, G.2
  • 47
    • 0028889436 scopus 로고
    • Interaction between focal adhesion kinase and Crk-associated tyrosine kinase substrate p130Cas
    • Polte, T. R., and Hanks, S. K. (1995). Interaction between focal adhesion kinase and Crk-associated tyrosine kinase substrate p130Cas. Proc. Nat. Acad. Sci. USA 92, 10678-10682.
    • (1995) Proc. Nat. Acad. Sci. USA , vol.92 , pp. 10678-10682
    • Polte, T.R.1    Hanks, S.K.2
  • 48
    • 0033200353 scopus 로고    scopus 로고
    • A putative exchange factor for Rho1 GTPase is required for initiation of cytokinesis in Drosophila
    • Prokopenko, S. N., Brumby, A., O'Keefe, L., Prior, L., He, Y., Saint, R., and Bellen, H. J. (1999). A putative exchange factor for Rho1 GTPase is required for initiation of cytokinesis in Drosophila. Genes Dev. 13, 2301-2314.
    • (1999) Genes Dev. , vol.13 , pp. 2301-2314
    • Prokopenko, S.N.1    Brumby, A.2    O'Keefe, L.3    Prior, L.4    He, Y.5    Saint, R.6    Bellen, H.J.7
  • 49
    • 0033989053 scopus 로고    scopus 로고
    • Tissue distribution of PEBBLE RNA and pebble protein during Drosophila embryonic development
    • Prokopenko, S. N., Saint, R., and Bellen, H. J. (2000). Tissue distribution of PEBBLE RNA and pebble protein during Drosophila embryonic development. Mech. Dev. 90, 269-273.
    • (2000) Mech. Dev. , vol.90 , pp. 269-273
    • Prokopenko, S.N.1    Saint, R.2    Bellen, H.J.3
  • 50
    • 27144495462 scopus 로고    scopus 로고
    • The focal adhesion scaffolding protein HEF1 regulates activation of the Aurora-A and Nek2 kinases at the centrosome
    • Pugacheva, E. N., and Golemis, E. A. (2005). The focal adhesion scaffolding protein HEF1 regulates activation of the Aurora-A and Nek2 kinases at the centrosome. Nat. Cell Biol. 7, 937-946.
    • (2005) Nat. Cell Biol. , vol.7 , pp. 937-946
    • Pugacheva, E.N.1    Golemis, E.A.2
  • 51
    • 0037166933 scopus 로고    scopus 로고
    • The roles of Fzy/Cdc20 and Fzr/Cd1 in regulating the destruction of cyclin B in space and time
    • Raff, J. W., Jeffers, K., and Huang, J. Y. (2002). The roles of Fzy/Cdc20 and Fzr/Cd1 in regulating the destruction of cyclin B in space and time. J. Cell Biol. 157, 1139-1149.
    • (2002) J. Cell Biol. , vol.157 , pp. 1139-1149
    • Raff, J.W.1    Jeffers, K.2    Huang, J.Y.3
  • 52
    • 0033731010 scopus 로고    scopus 로고
    • Focal adhesion kinase suppresses Rho activity to promote focal adhesion turnover
    • Ren, X. D., Kiosses, W. B., Sieg, D. J., Otey, C. A., Schlaepfer, D. D., and Schwartz, M. A. (2000). Focal adhesion kinase suppresses Rho activity to promote focal adhesion turnover. J. Cell Sci. 113, 3673-3678.
    • (2000) J. Cell Sci. , vol.113 , pp. 3673-3678
    • Ren, X.D.1    Kiosses, W.B.2    Sieg, D.J.3    Otey, C.A.4    Schlaepfer, D.D.5    Schwartz, M.A.6
  • 53
    • 0034865456 scopus 로고    scopus 로고
    • Rho GTPases and cell migration
    • Ridley, A. J. (2001). Rho GTPases and cell migration. J. Cell Sci. 114, 2713-2722.
    • (2001) J. Cell Sci. , vol.114 , pp. 2713-2722
    • Ridley, A.J.1
  • 54
    • 0026778133 scopus 로고
    • The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors
    • Ridley, A. J., and Hall, A. (1992). The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors. Cell 70, 389-399.
    • (1992) Cell , vol.70 , pp. 389-399
    • Ridley, A.J.1    Hall, A.2
  • 55
    • 10744225152 scopus 로고    scopus 로고
    • Deregulation and mislocalization of the cytokinesis regulator ECT2 activate the Rho signaling pathways leading to malignant transformation
    • Saito, S., et al. (2004). Deregulation and mislocalization of the cytokinesis regulator ECT2 activate the Rho signaling pathways leading to malignant transformation. J. Biol. Chem. 279, 7169-7179.
    • (2004) J. Biol. Chem. , vol.279 , pp. 7169-7179
    • Saito, S.1
  • 56
    • 0242526719 scopus 로고    scopus 로고
    • Rho exchange factor ECT2 is induced by growth factors and regulates cytokinesis through the N-terminal cell cycle regulator-related domains
    • Saito, S., Tatsumoto, T., Lorenzi, M. V., Chedid, M., Kapoor, V., Sakata, H., Rubin, J., and Miki, T. (2003). Rho exchange factor ECT2 is induced by growth factors and regulates cytokinesis through the N-terminal cell cycle regulator-related domains. J. Cell. Biochem. 90, 819-836.
    • (2003) J. Cell. Biochem. , vol.90 , pp. 819-836
    • Saito, S.1    Tatsumoto, T.2    Lorenzi, M.V.3    Chedid, M.4    Kapoor, V.5    Sakata, H.6    Rubin, J.7    Miki, T.8
  • 57
    • 0027990414 scopus 로고
    • A novel signaling molecule, p130, forms stable complexes in vivo with v-Crk and v-Src in a tyrosine phosphorylation-dependent manner
    • Sakai, R., Iwamatsu, A., Hirano, N., Ogawa, S., Tanaka, T., Mano, H., Yazaki, Y., and Hirai, H. (1994). A novel signaling molecule, p130, forms stable complexes in vivo with v-Crk and v-Src in a tyrosine phosphorylation-dependent manner. EMBO J. 13, 3748-3756.
    • (1994) EMBO J. , vol.13 , pp. 3748-3756
    • Sakai, R.1    Iwamatsu, A.2    Hirano, N.3    Ogawa, S.4    Tanaka, T.5    Mano, H.6    Yazaki, Y.7    Hirai, H.8
  • 58
    • 0030889320 scopus 로고    scopus 로고
    • Characterization of the kinase activity essential for tyrosine phosphorylation of p130Cas in fibroblasts
    • Sakai, R., Nakamoto, T., Ozawa, K., Aizawa, S., and Hirai, H. (1997). Characterization of the kinase activity essential for tyrosine phosphorylation of p130Cas in fibroblasts. Oncogene 14, 1419-1426.
    • (1997) Oncogene , vol.14 , pp. 1419-1426
    • Sakai, R.1    Nakamoto, T.2    Ozawa, K.3    Aizawa, S.4    Hirai, H.5
  • 59
    • 0032952209 scopus 로고    scopus 로고
    • Cleavage furrows formed between centrosomes lacking an intervening spindle and chromosomes contain microtubule bundles, INCENP, and CHO1 but not CENP-E
    • Savoian, M. S., Earnshaw, W. C., Khodjakov, A., and Rieder, C. L. (1999). Cleavage furrows formed between centrosomes lacking an intervening spindle and chromosomes contain microtubule bundles, INCENP, and CHO1 but not CENP-E. Mol. Biol. Cell 10, 297-311.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 297-311
    • Savoian, M.S.1    Earnshaw, W.C.2    Khodjakov, A.3    Rieder, C.L.4
  • 61
    • 0030661566 scopus 로고    scopus 로고
    • Integrins, oncogenes, and anchorage independence
    • Schwartz, M. A. (1997). Integrins, oncogenes, and anchorage independence. J. Cell Biol. 139, 575-578.
    • (1997) J. Cell Biol. , vol.139 , pp. 575-578
    • Schwartz, M.A.1
  • 62
    • 0034256024 scopus 로고    scopus 로고
    • Signaling networks linking integrins and rho family GTPases
    • Schwartz, M. A., and Shattil, S. J. (2000). Signaling networks linking integrins and rho family GTPases. Trends Biochem. Sci. 25, 388-391.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 388-391
    • Schwartz, M.A.1    Shattil, S.J.2
  • 63
    • 0034955193 scopus 로고    scopus 로고
    • Y-27632, an inhibitor of Rho-associated kinases, prevents tyrosine phosphorylation of focal adhesion kinase and paxillin induced by bombesin: Dissociation from tyrosine phosphorylation of p130(CAS)
    • Sinnett-Smith, J., Lunn, J. A., Leopoldt, D., and Rozengurt, E. (2001). Y-27632, an inhibitor of Rho-associated kinases, prevents tyrosine phosphorylation of focal adhesion kinase and paxillin induced by bombesin: dissociation from tyrosine phosphorylation of p130(CAS). Exp. Cell Res. 266, 292-302.
    • (2001) Exp. Cell Res. , vol.266 , pp. 292-302
    • Sinnett-Smith, J.1    Lunn, J.A.2    Leopoldt, D.3    Rozengurt, E.4
  • 64
    • 2942554939 scopus 로고    scopus 로고
    • Requirement for C-terminal sequences in regulation of Ect2 guanine nucleotide exchange specificity and transformation
    • Solski, P. A., Wilder, R. S., Rossman, K. L., Sondek, J., Cox, A. D., Campbell, S. L., and Der, C. J. (2004). Requirement for C-terminal sequences in regulation of Ect2 guanine nucleotide exchange specificity and transformation. J. Biol. Chem. 279, 25226-25233.
    • (2004) J. Biol. Chem. , vol.279 , pp. 25226-25233
    • Solski, P.A.1    Wilder, R.S.2    Rossman, K.L.3    Sondek, J.4    Cox, A.D.5    Campbell, S.L.6    Der, C.J.7
  • 65
    • 0344586105 scopus 로고    scopus 로고
    • Potential roles of the nucleotide exchange factor ECT2 and Cdc42 GTPase in spindle assembly in Xenopus egg cell-free extracts
    • Tatsumoto, T., Sakata, H., Dasso, M., and Mild, T. (2003). Potential roles of the nucleotide exchange factor ECT2 and Cdc42 GTPase in spindle assembly in Xenopus egg cell-free extracts. J. Cell. Biochem. 90, 892-900.
    • (2003) J. Cell. Biochem. , vol.90 , pp. 892-900
    • Tatsumoto, T.1    Sakata, H.2    Dasso, M.3    Mild, T.4
  • 66
    • 0033615978 scopus 로고    scopus 로고
    • Human ECT2 is an exchange factor for Rho GTPases, phosphorylated in G2/M phases, and involved in cytokinesis
    • Tatsumoto, T., Xie, X., Blumenthal, R., Okamoto, I., and Miki, T. (1999). Human ECT2 is an exchange factor for Rho GTPases, phosphorylated in G2/M phases, and involved in cytokinesis. J. Cell Biol. 147, 921-928.
    • (1999) J. Cell Biol. , vol.147 , pp. 921-928
    • Tatsumoto, T.1    Xie, X.2    Blumenthal, R.3    Okamoto, I.4    Miki, T.5
  • 67
    • 0030968580 scopus 로고    scopus 로고
    • Rho GTPases and signaling networks
    • Van Aelst, L., and D'Souza-Schorey, C. (1997). Rho GTPases and signaling networks. Genes Dev. 11, 2295-2322.
    • (1997) Genes Dev. , vol.11 , pp. 2295-2322
    • Van Aelst, L.1    D'Souza-Schorey, C.2
  • 69
    • 0029664531 scopus 로고    scopus 로고
    • Induction of p130Cas signaling complex formation upon integrin-mediated cell adhesion: A role for Src family kinases
    • Vuori, K., Hirai, H., Aizawa, S., and Ruoslahti, E. (1996). Induction of p130Cas signaling complex formation upon integrin-mediated cell adhesion: a role for Src family kinases. Mol. Cell. Biol. 16, 2606-2613.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 2606-2613
    • Vuori, K.1    Hirai, H.2    Aizawa, S.3    Ruoslahti, E.4
  • 70
    • 0030661929 scopus 로고    scopus 로고
    • Mitosis specific serine phosphorylation and downregulation of one of the focal adhesion protein, paxillin
    • Yamaguchi, R., Mazaki, Y., Hirota, K., Hashimoto, S., and Sabe, H. (1997). Mitosis specific serine phosphorylation and downregulation of one of the focal adhesion protein, paxillin. Oncogene 15, 1753-1761.
    • (1997) Oncogene , vol.15 , pp. 1753-1761
    • Yamaguchi, R.1    Mazaki, Y.2    Hirota, K.3    Hashimoto, S.4    Sabe, H.5
  • 71
    • 0033601745 scopus 로고    scopus 로고
    • Dissociation of FAK/p130(CAS)/c-Src complex during mitosis: Role of mitosis-specific serine phosphorylation of FAK
    • Yamakita, Y., Totsukawa, G., Yamashiro, S., Fry, D., Zhang, X., Hanks, S. K., and Matsumura, F. (1999). Dissociation of FAK/p130(CAS)/c-Src complex during mitosis: role of mitosis-specific serine phosphorylation of FAK. J. Cell Biol. 244, 315-324.
    • (1999) J. Cell Biol. , vol.244 , pp. 315-324
    • Yamakita, Y.1    Totsukawa, G.2    Yamashiro, S.3    Fry, D.4    Zhang, X.5    Hanks, S.K.6    Matsumura, F.7
  • 72
    • 0037088609 scopus 로고    scopus 로고
    • Members of the zyxin family of LIM proteins interact with members of the p130cas family of signal transducers
    • Yi, J., Kloeker, S., Jensen, C. C., Bockholt, S., Honda, H., Hirai, H., and Beckerle, M. C. (2002). Members of the zyxin family of LIM proteins interact with members of the p130cas family of signal transducers. J. Biol. Chem. 277, 9580-9589.
    • (2002) J. Biol. Chem. , vol.277 , pp. 9580-9589
    • Yi, J.1    Kloeker, S.2    Jensen, C.C.3    Bockholt, S.4    Honda, H.5    Hirai, H.6    Beckerle, M.C.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.