메뉴 건너뛰기




Volumn 19, Issue 3, 1999, Pages 1784-1799

The Gab1 PH domain is required for localization of Gab1 at sites of cell-cell contact and epithelial morphogenesis downstream from the Met receptor tyrosine kinase

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN TYROSINE KINASE; SCATTER FACTOR; SCATTER FACTOR RECEPTOR;

EID: 0033020148     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.19.3.1784     Document Type: Article
Times cited : (180)

References (82)
  • 1
    • 0024601010 scopus 로고
    • PDGF-dependent tyrosine phosphorylation stimulates production of novel polyphosphoinositides in intact cells
    • Auger, K. R., L. A. Serunian, S. P. Soltoff, P. Libby, and L. C. Cantley. 1989. PDGF-dependent tyrosine phosphorylation stimulates production of novel polyphosphoinositides in intact cells. Cell 57:167-175.
    • (1989) Cell , vol.57 , pp. 167-175
    • Auger, K.R.1    Serunian, L.A.2    Soltoff, S.P.3    Libby, P.4    Cantley, L.C.5
  • 3
    • 0031577691 scopus 로고    scopus 로고
    • Gab1 coupling to the HGF/Met receptor multifunctional docking site requires binding of Grb2 and correlates with the transforming potential
    • Bardelli, A., P. Longati, D. Gramaglia, M. C. Stella, and P. M. Comoglio. 1997. Gab1 coupling to the HGF/Met receptor multifunctional docking site requires binding of Grb2 and correlates with the transforming potential. Oncogene 15:3103-3111.
    • (1997) Oncogene , vol.15 , pp. 3103-3111
    • Bardelli, A.1    Longati, P.2    Gramaglia, D.3    Stella, M.C.4    Comoglio, P.M.5
  • 4
    • 0028268338 scopus 로고
    • Creation of an hepatocyte growth factor/scatter factor autocrine loop in carcinoma cells induces invasive properties associated with increased tumorigenicity
    • Bellusci, S., G. Moens, G. Gaudino, P. Comoglio, T. Nakamura, J. P. Thiery, and J. Jouanneau. 1994. Creation of an hepatocyte growth factor/scatter factor autocrine loop in carcinoma cells induces invasive properties associated with increased tumorigenicity. Oncogene 9:1091-1099.
    • (1994) Oncogene , vol.9 , pp. 1091-1099
    • Bellusci, S.1    Moens, G.2    Gaudino, G.3    Comoglio, P.4    Nakamura, T.5    Thiery, J.P.6    Jouanneau, J.7
  • 6
    • 0031459864 scopus 로고    scopus 로고
    • p62dok: A constitutively tyrosine-phosphorylated. GAP-associated protein in chronic myelogenous leukemia progenitor cells
    • Carpino, N., D. Wisniewski, A. Strife, D. Marshak, R. Kobayashi, B. Stillman, and B. Clarkson. 1997. p62dok: A constitutively tyrosine-phosphorylated. GAP-associated protein in chronic myelogenous leukemia progenitor cells. Cell 88:197-204.
    • (1997) Cell , vol.88 , pp. 197-204
    • Carpino, N.1    Wisniewski, D.2    Strife, A.3    Marshak, D.4    Kobayashi, R.5    Stillman, B.6    Clarkson, B.7
  • 7
    • 0031002348 scopus 로고    scopus 로고
    • The role of the PH domain in the signal-dependent membrane targeting of Sos
    • Chen, R. H., S. Corbalan-Garcia, and D. Bar-Sagi. 1997. The role of the PH domain in the signal-dependent membrane targeting of Sos. EMBO J. 16: 1351-1359.
    • (1997) EMBO J. , vol.16 , pp. 1351-1359
    • Chen, R.H.1    Corbalan-Garcia, S.2    Bar-Sagi, D.3
  • 8
    • 0028814087 scopus 로고
    • HGF-mediated chemotaxis and tubulogenesis require activation of the phosphatidylinositol 3-kinase
    • Derman, M. P., M. J. Cunha, E. J. Barros, S. K. Nigam, and L. G. Cantley. 1995. HGF-mediated chemotaxis and tubulogenesis require activation of the phosphatidylinositol 3-kinase. Am. J. Physiol. 268:1211-1217.
    • (1995) Am. J. Physiol. , vol.268 , pp. 1211-1217
    • Derman, M.P.1    Cunha, M.J.2    Barros, E.J.3    Nigam, S.K.4    Cantley, L.G.5
  • 9
    • 0001517943 scopus 로고    scopus 로고
    • Hepatocyte growth factor/scatter factor is an axonal chemoattractant and a neurotrophic factor for spinal motor neurons
    • Ebens, A., K. Brose, E. D. Leonardo, M. G. Jr. Hanson, F. Bladt, C. Birchmeier, B. A. Barres, and M. Tessier-Lavigne. 1996. Hepatocyte growth factor/scatter factor is an axonal chemoattractant and a neurotrophic factor for spinal motor neurons. Neuron 17:1157-1172.
    • (1996) Neuron , vol.17 , pp. 1157-1172
    • Ebens, A.1    Brose, K.2    Leonardo, E.D.3    Hanson M.G., Jr.4    Bladt, F.5    Birchmeier, C.6    Barres, B.A.7    Tessier-Lavigne, M.8
  • 10
    • 0032518666 scopus 로고
    • Activation of phospholipase Cγ by PI 3-kinase-induced PH domain-mediated membrane targeting
    • Falasca, M., S. K. Logan, V. P. Lehto, G. Baccante, M. A. Lemmon, and J. Schlessinger. 1988. Activation of phospholipase Cγ by PI 3-kinase-induced PH domain-mediated membrane targeting. EMBO J. 17:414-422.
    • (1988) EMBO J. , vol.17 , pp. 414-422
    • Falasca, M.1    Logan, S.K.2    Lehto, V.P.3    Baccante, G.4    Lemmon, M.A.5    Schlessinger, J.6
  • 11
    • 0027349034 scopus 로고
    • Signal transduction in c-met mediated motogenesis. Hepatocyte growth factor: Scatter factor
    • Faletto, D. L., D. R. Kaplan, D. O. Halverson, E. M. Rosen, and G. F. Vande Woude. 1993. Signal transduction in c-met mediated motogenesis. Hepatocyte growth factor: scatter factor. EXS 65:107-130.
    • (1993) EXS , vol.65 , pp. 107-130
    • Faletto, D.L.1    Kaplan, D.R.2    Halverson, D.O.3    Rosen, E.M.4    Vande Woude, G.F.5
  • 12
    • 0029617615 scopus 로고
    • Structure of the high affinity complex of inositol triphosphate with a phospholipase C pleckstrin homology domain
    • Ferguson, K. M., M. A. Lemmon, J. Schlessinger, and P. B. Sigler. 1995. Structure of the high affinity complex of inositol triphosphate with a phospholipase C pleckstrin homology domain. Cell 83:1037-1046.
    • (1995) Cell , vol.83 , pp. 1037-1046
    • Ferguson, K.M.1    Lemmon, M.A.2    Schlessinger, J.3    Sigler, P.B.4
  • 13
    • 17544371922 scopus 로고    scopus 로고
    • Pathways downstream of Shc and Grb2 are required for cell transformation by the Tpr-Met oncoprotein
    • Fixman, E. D., T. M. Fournier, D. M. Kamikura, M. A. Naujokas, and M. Park. 1996. Pathways downstream of Shc and Grb2 are required for cell transformation by the Tpr-Met oncoprotein. J. Biol. Chem. 271: 13116-13122.
    • (1996) J. Biol. Chem. , vol.271 , pp. 13116-13122
    • Fixman, E.D.1    Fournier, T.M.2    Kamikura, D.M.3    Naujokas, M.A.4    Park, M.5
  • 14
    • 0030839876 scopus 로고    scopus 로고
    • Efficient cellular transformation by the Met oncoprotein requires a functional Grb2 binding site and correlates with phosphorylation of the Grb2-associated proteins Cb1 and Gab1
    • Fixman, E. D., M. Holgado-Madruga, L. Nguyen, D. M. Kamikura, T. M. Fournier, A. J. Wong, and M. Park. 1997. Efficient cellular transformation by the Met oncoprotein requires a functional Grb2 binding site and correlates with phosphorylation of the Grb2-associated proteins Cb1 and Gab1. J. Biol. Chem. 272:20167-20172.
    • (1997) J. Biol. Chem. , vol.272 , pp. 20167-20172
    • Fixman, E.D.1    Holgado-Madruga, M.2    Nguyen, L.3    Kamikura, D.M.4    Fournier, T.M.5    Wong, A.J.6    Park, M.7
  • 15
    • 0028816813 scopus 로고
    • Efficient cell transformation by the Tpr-Met oncoprotein is dependent upon tyrosine 489 in the carboxy-terminus
    • Fixman, E. D., M. A. Naujokas, G. A. Rodrigues, M. F. Moran, and M. Park. 1995. Efficient cell transformation by the Tpr-Met oncoprotein is dependent upon tyrosine 489 in the carboxy-terminus. Oncogene 10:237-249.
    • (1995) Oncogene , vol.10 , pp. 237-249
    • Fixman, E.D.1    Naujokas, M.A.2    Rodrigues, G.A.3    Moran, M.F.4    Park, M.5
  • 17
    • 0029809118 scopus 로고    scopus 로고
    • Branching tubulogenesis, but not scatter of Madin-Darby canine kidney cells requires a functional Grb2 binding site in the Met receptor tyrosine kinase
    • Fournier, T., D. Kamikura, K. Teng, and M. Park. 1996. Branching tubulogenesis, but not scatter of Madin-Darby canine kidney cells requires a functional Grb2 binding site in the Met receptor tyrosine kinase. J. Biol. Chem. 271:22211-22217.
    • (1996) J. Biol. Chem. , vol.271 , pp. 22211-22217
    • Fournier, T.1    Kamikura, D.2    Teng, K.3    Park, M.4
  • 18
    • 0031039024 scopus 로고    scopus 로고
    • Direct regulation of the Akt proto-oncogene product by phosphatidylinositol-3,4-bisphosphate
    • Franke, T. F., D. R. Kaplan, L. C. Cantley, and A. Toker. 1997. Direct regulation of the Akt proto-oncogene product by phosphatidylinositol-3,4-bisphosphate. Science 275:665-668.
    • (1997) Science , vol.275 , pp. 665-668
    • Franke, T.F.1    Kaplan, D.R.2    Cantley, L.C.3    Toker, A.4
  • 19
    • 0030991386 scopus 로고    scopus 로고
    • High affinity binding of inositol phosphates and phosphoinositides to the pleckstrin homology domain of RAC/protein kinase B and their influence on kinase activity
    • Frech, M., M. Andjelkovic, E. Ingley, K. K. Reddy, J. R. Falck, and B. A. Hemmings. 1997. High affinity binding of inositol phosphates and phosphoinositides to the pleckstrin homology domain of RAC/protein kinase B and their influence on kinase activity. J. Biol. Chem. 272:84474-84481.
    • (1997) J. Biol. Chem. , vol.272 , pp. 84474-84481
    • Frech, M.1    Andjelkovic, M.2    Ingley, E.3    Reddy, K.K.4    Falck, J.R.5    Hemmings, B.A.6
  • 20
    • 0028787055 scopus 로고
    • The pleckstrin homology domain of phospholipase C-δ1 binds with high affinity to phosphatidylinositol 4,5-biphosphate in bilayer membranes
    • Garcia, P., R. Gupta, S. Shah, A. J. Morris, S. A. Rudge, S. Scarlata, V. Petrova, S. McLaughlin, and M. J. Rebecchi. 1995. The pleckstrin homology domain of phospholipase C-δ1 binds with high affinity to phosphatidylinositol 4,5-biphosphate in bilayer membranes. Biochemistry 34:16228-16234.
    • (1995) Biochemistry , vol.34 , pp. 16228-16234
    • Garcia, P.1    Gupta, R.2    Shah, S.3    Morris, A.J.4    Rudge, S.A.5    Scarlata, S.6    Petrova, V.7    McLaughlin, S.8    Rebecchi, M.J.9
  • 23
    • 0028021882 scopus 로고
    • Pleckstrin homology domains bind to phosphatidylinositol 4,5-bisphosphate
    • Harlan, J. E., P. J. Hajduk, H. S. Yoon, and S. W. Fesik. 1994. Pleckstrin homology domains bind to phosphatidylinositol 4,5-bisphosphate. Nature 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
  • 24
    • 0030003293 scopus 로고    scopus 로고
    • Daughter of sevenless is a substrate of the phosphotyrosine phosphatase Corkscrew and functions during sevenless signaling
    • Herbst, R., P. M. Caroll, J. D. Allard, J. Schilling, T. Raabe, and M. A. Simon. 1996. Daughter of sevenless is a substrate of the phosphotyrosine phosphatase Corkscrew and functions during sevenless signaling. Cell 85: 899-909.
    • (1996) Cell , vol.85 , pp. 899-909
    • Herbst, R.1    Caroll, P.M.2    Allard, J.D.3    Schilling, J.4    Raabe, T.5    Simon, M.A.6
  • 25
    • 0030028790 scopus 로고    scopus 로고
    • A Grb2-associated docking protein in EGF- and insulin-receptor signaling
    • Holgado-Madruga, M., D. R. Emlet, D. K. Moscatello, A. K. Godwin, and A. J. Wong. 1996. A Grb2-associated docking protein in EGF- and insulin-receptor signaling. Nature 379:560-564.
    • (1996) Nature , vol.379 , pp. 560-564
    • Holgado-Madruga, M.1    Emlet, D.R.2    Moscatello, D.K.3    Godwin, A.K.4    Wong, A.J.5
  • 26
    • 0030812590 scopus 로고    scopus 로고
    • Grb2-associated binder-1 mediates phosphatidylinositol 3-kinase activation and the promotion of cell survival by nerve growth factor
    • Holgado-Madruga, M., D. K. Moscatello, D. R. Emlet, R. Dieterich, and A. J. Wong. 1997. Grb2-associated binder-1 mediates phosphatidylinositol 3-kinase activation and the promotion of cell survival by nerve growth factor. Proc. Natl. Acad. Sci. USA 94:12419-12424.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 12419-12424
    • Holgado-Madruga, M.1    Moscatello, D.K.2    Emlet, D.R.3    Dieterich, R.4    Wong, A.J.5
  • 29
    • 0028918408 scopus 로고
    • Ras-dependent induction of cellular responses by constitutively active phosphatidylinositol-3 kinase
    • Hu, Q., A. Klippel, A. J. Muslin, W. J. Fantl, and L. T. Williams. 1995. Ras-dependent induction of cellular responses by constitutively active phosphatidylinositol-3 kinase. Science 268:100-102.
    • (1995) Science , vol.268 , pp. 100-102
    • Hu, Q.1    Klippel, A.2    Muslin, A.J.3    Fantl, W.J.4    Williams, L.T.5
  • 31
    • 0026010993 scopus 로고
    • Hepatocyte growth factor/hepatopoietin A stimulates the growth of rat kidney proximal tubule epithelial cells (RPTE), rat nonparenchymal liver cells, human melanoma cells, mouse keratinocytes and stimulates anchorage-independent growth of SV-40 transformed RPTE
    • Kan, M., G. Zhang, R. Zarnegar, G. Michalopoulos, Y. Myoken, W. L. McKeehan, and J. I. Stevens. 1991. Hepatocyte growth factor/hepatopoietin A stimulates the growth of rat kidney proximal tubule epithelial cells (RPTE), rat nonparenchymal liver cells, human melanoma cells, mouse keratinocytes and stimulates anchorage-independent growth of SV-40 transformed RPTE. Biochem. Biophys. Res. Commun. 174:331-337.
    • (1991) Biochem. Biophys. Res. Commun. , vol.174 , pp. 331-337
    • Kan, M.1    Zhang, G.2    Zarnegar, R.3    Michalopoulos, G.4    Myoken, Y.5    McKeehan, W.L.6    Stevens, J.I.7
  • 32
    • 0032563207 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinase induces scattering and tubulogenesis in epithelial cells through a novel pathway
    • Khwaja, A., K. Lehmann, B. M. Marte, and J. Downward. 1998. Phosphoinositide 3-kinase induces scattering and tubulogenesis in epithelial cells through a novel pathway. J. Biol. Chem. 273:18793-18801.
    • (1998) J. Biol. Chem. , vol.273 , pp. 18793-18801
    • Khwaja, A.1    Lehmann, K.2    Marte, B.M.3    Downward, J.4
  • 33
    • 0028198330 scopus 로고
    • The interaction of small domains between the subunits of phosphatidylinositol 3-kinase determines enzyme activity
    • Klippel, A., J. A. Escobedo, M. Hirano, and L. T. Williams. 1994. The interaction of small domains between the subunits of phosphatidylinositol 3-kinase determines enzyme activity. Mol. Cell. Biol. 14:2675-2685.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 2675-2685
    • Klippel, A.1    Escobedo, J.A.2    Hirano, M.3    Williams, L.T.4
  • 34
    • 0027264590 scopus 로고
    • The cell dissociation and motility triggered by scatter factor/hepatocyte growth factor are mediated through the cytoplasmic domain of the c-Met receptor
    • Komada, M., and N. Kitamura. 1993. The cell dissociation and motility triggered by scatter factor/hepatocyte growth factor are mediated through the cytoplasmic domain of the c-Met receptor. Oncogene 8:2381-2390.
    • (1993) Oncogene , vol.8 , pp. 2381-2390
    • Komada, M.1    Kitamura, N.2
  • 35
    • 0028670203 scopus 로고
    • The pleckstrin homology domain of RAC protein kinase associates with the regulatory domain of protein kinase Cζ
    • Konishi, H., S. Kuroda, and U. Kikkawa. 1994. The pleckstrin homology domain of RAC protein kinase associates with the regulatory domain of protein kinase Cζ. Biochem. Biophys. Res. Commun. 205:1770-1775.
    • (1994) Biochem. Biophys. Res. Commun. , vol.205 , pp. 1770-1775
    • Konishi, H.1    Kuroda, S.2    Kikkawa, U.3
  • 36
    • 0031006326 scopus 로고    scopus 로고
    • Regulatory recruitment of signaling molecules to the cell membrane by pleckstrin homology domains
    • Lemmon, M. A., M. Falasca, K. M. Ferguson, and J. Schlessinger. 1997. Regulatory recruitment of signaling molecules to the cell membrane by pleckstrin homology domains. Trends Cell Biol. 7:237-242.
    • (1997) Trends Cell Biol. , vol.7 , pp. 237-242
    • Lemmon, M.A.1    Falasca, M.2    Ferguson, K.M.3    Schlessinger, J.4
  • 37
    • 0028874438 scopus 로고
    • Specific and high-affinity binding of inositol phosphates to an isolated pleckstrin homology domain
    • Lemmon, M. A., K. M. Ferguson, R. O'Brien, P. B. Sigler, and J. Schlessinger. 1995. Specific and high-affinity binding of inositol phosphates to an isolated pleckstrin homology domain. Proc. Natl. Acad. Sci. USA 92:10472-10476.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 10472-10476
    • Lemmon, M.A.1    Ferguson, K.M.2    O'Brien, R.3    Sigler, P.B.4    Schlessinger, J.5
  • 38
    • 0029939448 scopus 로고    scopus 로고
    • PH domains: Diverse sequences with a common fold recruit signaling molecules to the cell surface
    • Lemmon, M. A., K. M. Ferguson, and J. Schlessinger. 1996. PH domains: diverse sequences with a common fold recruit signaling molecules to the cell surface. Cell 85:621-624.
    • (1996) Cell , vol.85 , pp. 621-624
    • Lemmon, M.A.1    Ferguson, K.M.2    Schlessinger, J.3
  • 39
    • 0031440947 scopus 로고    scopus 로고
    • Met receptor signaling is required for sensory nerve development and HGF promotes axonal growth and survival of sensory neurones
    • Maina, F., M. C. Hilton, C. Ponzetto, A. M. Davies, and R. Klein. 1997. Met receptor signaling is required for sensory nerve development and HGF promotes axonal growth and survival of sensory neurones. Genes Dev. 11: 3341-3350.
    • (1997) Genes Dev. , vol.11 , pp. 3341-3350
    • Maina, F.1    Hilton, M.C.2    Ponzetto, C.3    Davies, A.M.4    Klein, R.5
  • 40
    • 0028872649 scopus 로고
    • Specificity of receptor tyrosine kinase signaling: Transient versus sustained extracellular signal-regulated kinase activation
    • Marshall, C. J. 1995. Specificity of receptor tyrosine kinase signaling: transient versus sustained extracellular signal-regulated kinase activation. Cell 80:179-185.
    • (1995) Cell , vol.80 , pp. 179-185
    • Marshall, C.J.1
  • 41
    • 0027344558 scopus 로고
    • Roles of HGF as a pleiotropic factor in organ regeneration
    • Matsumoto, K., and T. S. Nakamura. 1993. Roles of HGF as a pleiotropic factor in organ regeneration. EXS 65:225-249.
    • (1993) EXS , vol.65 , pp. 225-249
    • Matsumoto, K.1    Nakamura, T.S.2
  • 42
    • 0030931216 scopus 로고    scopus 로고
    • Regulated membrane localization of Tiam1, mediated by the NH2-terminal pleckstrin homology domain, is required for Rac-dependent membrane ruffling and C-Jun NH2-terminal kinase activation
    • Michiels, F., J. C. Stam, P. L. Hordijk, R. A. van der Kammen, L. RuulsvanStalle, C. A. Feltkamp, and J. G. Collard. 1997. Regulated membrane localization of Tiam1, mediated by the NH2-terminal pleckstrin homology domain, is required for Rac-dependent membrane ruffling and C-Jun NH2-terminal kinase activation. J. Cell Biol. 137:387-398.
    • (1997) J. Cell Biol. , vol.137 , pp. 387-398
    • Michiels, F.1    Stam, J.C.2    Hordijk, P.L.3    Van Der Kammen, R.A.4    Ruulsvanstalle, L.5    Feltkamp, C.A.6    Collard, J.G.7
  • 43
    • 0025825990 scopus 로고
    • Induction of epithelial tubular morphogenesis in vitro by fibroblast-derived soluble factors
    • Montesano, R., G. Schaller, and L. Orci. 1991. Induction of epithelial tubular morphogenesis in vitro by fibroblast-derived soluble factors. Cell 66:697-711.
    • (1991) Cell , vol.66 , pp. 697-711
    • Montesano, R.1    Schaller, G.2    Orci, L.3
  • 45
    • 0026287917 scopus 로고
    • Structure and function of hepatocyte growth factor
    • Nakamura, T. 1991. Structure and function of hepatocyte growth factor. Prog. Growth Factor Res. 3:67-85.
    • (1991) Prog. Growth Factor Res. , vol.3 , pp. 67-85
    • Nakamura, T.1
  • 46
    • 0030843307 scopus 로고    scopus 로고
    • Association of the multisubstrate docking protein Gab1 with the hepatocyte growth factor receptor requires a functional Grb2 binding site involving tyrosine 1356
    • Nguyen, L., M. Holgado-Madruga, C. Maroun, E. D. Fixman, D. Kamikura, T. Fournier, A. Charest, M. L. Tremblay, A. J. Wong, and M. Park. 1997. Association of the multisubstrate docking protein Gab1 with the hepatocyte growth factor receptor requires a functional Grb2 binding site involving tyrosine 1356. J. Biol. Chem. 272:20811-20819.
    • (1997) J. Biol. Chem. , vol.272 , pp. 20811-20819
    • Nguyen, L.1    Holgado-Madruga, M.2    Maroun, C.3    Fixman, E.D.4    Kamikura, D.5    Fournier, T.6    Charest, A.7    Tremblay, M.L.8    Wong, A.J.9    Park, M.10
  • 47
    • 0024383949 scopus 로고
    • Regulation of desmosome assembly in epithelial cells: Kinetics of synthesis, transport, and stabilization of desmoglein I, a major protein of the membrane core domain
    • Pasdar, M., and W. J. Nelson. 1989. Regulation of desmosome assembly in epithelial cells: kinetics of synthesis, transport, and stabilization of desmoglein I, a major protein of the membrane core domain. J. Cell Biol. 109: 163-177.
    • (1989) J. Cell Biol. , vol.109 , pp. 163-177
    • Pasdar, M.1    Nelson, W.J.2
  • 49
    • 0028859279 scopus 로고
    • Protein modules and signaling networks
    • Pawson, T. 1995. Protein modules and signaling networks. Nature 373:573-580.
    • (1995) Nature , vol.373 , pp. 573-580
    • Pawson, T.1
  • 50
    • 0028351702 scopus 로고
    • A multifunctional docking site mediates signaling and transformation by the hepatocyte growth factor/scatter factor receptor family
    • Ponzetto, C., A. Bardelli, Z. Zhen, F. Maina, P. dalla Zonca, S. Giordano, A. Graziani, G. Panayotou, and P. M. Comoglio. 1994. A multifunctional docking site mediates signaling and transformation by the hepatocyte growth factor/scatter factor receptor family. Cell 77:261-271.
    • (1994) Cell , vol.77 , pp. 261-271
    • Ponzetto, C.1    Bardelli, A.2    Zhen, Z.3    Maina, F.4    Dalla Zonca, P.5    Giordano, S.6    Graziani, A.7    Panayotou, G.8    Comoglio, P.M.9
  • 51
    • 0029984739 scopus 로고    scopus 로고
    • DOS, a novel pleckstrin homology domain-containing protein required for signal transduction between sevenless and RAS1 in Drosophila
    • Raabe, T., J. Riesgo-Escovar, X. Liu, B. S. Bausenwein, P. Deak, P. Maroy, and E. Hafen. 1996. DOS, a novel pleckstrin homology domain-containing protein required for signal transduction between sevenless and RAS1 in Drosophila. Cell 85:911-920.
    • (1996) Cell , vol.85 , pp. 911-920
    • Raabe, T.1    Riesgo-Escovar, J.2    Liu, X.3    Bausenwein, B.S.4    Deak, P.5    Maroy, P.6    Hafen, E.7
  • 53
    • 0025881838 scopus 로고
    • Alternative splicing generates isoforms of the met receptor tyrosine kinase which undergo differential processing
    • Rodrigues, G. A., M. A. Naujokas, and M. Park. 1991. Alternative splicing generates isoforms of the met receptor tyrosine kinase which undergo differential processing. Mol. Cell. Biol. 11:2962-2970.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 2962-2970
    • Rodrigues, G.A.1    Naujokas, M.A.2    Park, M.3
  • 54
    • 0028301299 scopus 로고
    • Autophosphorylation modulates the kinase activity and oncogenic potential of the Met receptor tyrosine kinase
    • Rodrigues, G. A., and M. Park. 1994. Autophosphorylation modulates the kinase activity and oncogenic potential of the Met receptor tyrosine kinase. Oncogene 9:2019-2027.
    • (1994) Oncogene , vol.9 , pp. 2019-2027
    • Rodrigues, G.A.1    Park, M.2
  • 56
    • 0027318311 scopus 로고
    • A novel putative receptor protein tyrosine kinase of the met family
    • Ronsin, C., F. Muscatelli, M. G. Mattei, and R. Breathnach. 1993. A novel putative receptor protein tyrosine kinase of the met family. Oncogene 8:1195-1202.
    • (1993) Oncogene , vol.8 , pp. 1195-1202
    • Ronsin, C.1    Muscatelli, F.2    Mattei, M.G.3    Breathnach, R.4
  • 57
    • 0028850053 scopus 로고
    • Hepatocyte growth factor induced scatter of Madin-Darby canine kidney cells requires phosphatidylinositol 3-kinase
    • Royal, I., and M. Park. 1995. Hepatocyte growth factor induced scatter of Madin-Darby canine kidney cells requires phosphatidylinositol 3-kinase. J. Biol. Chem. 270:27780-27787.
    • (1995) J. Biol. Chem. , vol.270 , pp. 27780-27787
    • Royal, I.1    Park, M.2
  • 61
    • 0028919917 scopus 로고
    • Hepatocyte growth factor stimulates extensive development of branching duct-like structures by cloned mammary gland epithelial cells
    • Soriano, J. V., M. S. Pepper, T. Nakamura, L. Orci, and R. Montesano. 1995. Hepatocyte growth factor stimulates extensive development of branching duct-like structures by cloned mammary gland epithelial cells. J. Cell Sci. 108:413-430.
    • (1995) J. Cell Sci. , vol.108 , pp. 413-430
    • Soriano, J.V.1    Pepper, M.S.2    Nakamura, T.3    Orci, L.4    Montesano, R.5
  • 62
    • 0030723206 scopus 로고    scopus 로고
    • Targeting Tiam1 to the plasma membrane requires the cooperative function of the N-terminal pleckstrin homology domain and an adjacent protein interaction domain
    • Stam, J. C., E. E. Sander, F. Michiels, F. N. van Leeuwen, H. E. Kain, R. A. van der Kammen, and J. G. Collard. 1997. Targeting Tiam1 to the plasma membrane requires the cooperative function of the N-terminal pleckstrin homology domain and an adjacent protein interaction domain. J. Biol. Chem. 272:28447-28454.
    • (1997) J. Biol. Chem. , vol.272 , pp. 28447-28454
    • Stam, J.C.1    Sander, E.E.2    Michiels, F.3    Van Leeuwen, F.N.4    Kain, H.E.5    Van Der Kammen, R.A.6    Collard, J.G.7
  • 63
    • 0025731596 scopus 로고
    • Pathway of phophatidylinositol (3,4,5)-trisphosphate synthesis in activated neutrophils
    • Stephens, L. R., K. T. Hughes, and R. F. Irvine. 1991. Pathway of phophatidylinositol (3,4,5)-trisphosphate synthesis in activated neutrophils. Nature 351:33-39.
    • (1991) Nature , vol.351 , pp. 33-39
    • Stephens, L.R.1    Hughes, K.T.2    Irvine, R.F.3
  • 65
    • 0030718609 scopus 로고    scopus 로고
    • Regulation of cell-cell adhesion by Rac and Rho small G proteins in MDCK cells
    • Takaishi, K., T. Sasaki, H. Kotani, H. Nishioka, and Y. Takai. 1997. Regulation of cell-cell adhesion by Rac and Rho small G proteins in MDCK cells. J. Biol. Chem. 139:1047-1059.
    • (1997) J. Biol. Chem. , vol.139 , pp. 1047-1059
    • Takaishi, K.1    Sasaki, T.2    Kotani, H.3    Nishioka, H.4    Takai, Y.5
  • 67
    • 0028911690 scopus 로고
    • Placental defect and embryonic lethality in mice lacking hepatocyte growth factor/scatter factor
    • Uehara, Y., O. Minowa, C. Mori, K. Shiota, J. Kuno, T. Noda, and N. Kitamura. 1995. Placental defect and embryonic lethality in mice lacking hepatocyte growth factor/scatter factor. Nature 373:702-705.
    • (1995) Nature , vol.373 , pp. 702-705
    • Uehara, Y.1    Minowa, O.2    Mori, C.3    Shiota, K.4    Kuno, J.5    Noda, T.6    Kitamura, N.7
  • 68
    • 0032499031 scopus 로고    scopus 로고
    • Insulin-dependent translocation of ARNO to the plasma membrane of adipocytes requires phosphatidylinositol 3-kinase
    • Venkateswarlu, K., P. B. Oaty, J. M. Tavaré, and P. J. Cullen. 1998. Insulin-dependent translocation of ARNO to the plasma membrane of adipocytes requires phosphatidylinositol 3-kinase. Curr. Biol. 8:463-466.
    • (1998) Curr. Biol. , vol.8 , pp. 463-466
    • Venkateswarlu, K.1    Oaty, P.B.2    Tavaré, J.M.3    Cullen, P.J.4
  • 69
    • 0028170210 scopus 로고
    • A specific inhibitor of phosphatidylinositol 3-kinase, 2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one (LY294002)
    • Vlahos, C. J., W. F. Matter, K. Y. Hui, and R. F. Brown. 1994. A specific inhibitor of phosphatidylinositol 3-kinase, 2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one (LY294002). J. Biol. Chem. 269:5241-5248.
    • (1994) J. Biol. Chem. , vol.269 , pp. 5241-5248
    • Vlahos, C.J.1    Matter, W.F.2    Hui, K.Y.3    Brown, R.F.4
  • 70
    • 0030583283 scopus 로고    scopus 로고
    • The pleckstrin homology domain of human ßIΣII spectrin is targeted to the plasma membrane in vivo
    • Wang, D.-S., R. Miller, R. Shaw, and G. Shaw. 1996. The pleckstrin homology domain of human ßIΣII spectrin is targeted to the plasma membrane in vivo. Biochem. Biophys. Res. Commun. 225:420-426.
    • (1996) Biochem. Biophys. Res. Commun. , vol.225 , pp. 420-426
    • Wang, D.-S.1    Miller, R.2    Shaw, R.3    Shaw, G.4
  • 71
    • 0029855280 scopus 로고    scopus 로고
    • Interaction between Gab1 and c-Met receptor tyrosine kinase is responsible for epithelial morphogenesis
    • Weidner, K. M., S. Di Cesare, M. Sachs, V. Brinkmann, J. Behrens, and W. Birchmeier. 1996. Interaction between Gab1 and c-Met receptor tyrosine kinase is responsible for epithelial morphogenesis. Nature 384:173-176.
    • (1996) Nature , vol.384 , pp. 173-176
    • Weidner, K.M.1    Di Cesare, S.2    Sachs, M.3    Brinkmann, V.4    Behrens, J.5    Birchmeier, W.6
  • 72
    • 0027410889 scopus 로고
    • The Met receptor tyrosine kinase transduces motility, proliferation, and morphogenic signals of scatter factor/hepatocyte growth factor in epithelial cells
    • Weidner, K. M., M. Sachs, and W. Birchmeier. 1993. The Met receptor tyrosine kinase transduces motility, proliferation, and morphogenic signals of scatter factor/hepatocyte growth factor in epithelial cells. J. Cell Biol. 121: 145-154.
    • (1993) J. Cell Biol. , vol.121 , pp. 145-154
    • Weidner, K.M.1    Sachs, M.2    Birchmeier, W.3
  • 73
    • 0028940362 scopus 로고
    • Mutation of juxtamembrane tyrosine residue 1001 suppresses loss-of-function mutations of the met receptor in epithelial cells
    • Weidner, K. M., M. Sachs, D. Riethmacher, and W. Birchmeier. 1995. Mutation of juxtamembrane tyrosine residue 1001 suppresses loss-of-function mutations of the met receptor in epithelial cells. Proc. Natl. Acad. Sci. USA 92:2597-2601.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 2597-2601
    • Weidner, K.M.1    Sachs, M.2    Riethmacher, D.3    Birchmeier, W.4
  • 75
    • 0031444245 scopus 로고    scopus 로고
    • Identification of the Ab1- and ras-GAP-associated 62 kDa protein as a docking protein, Dok.
    • Yamanashi, Y., and D. Baltimore. 1997. Identification of the Ab1- and ras-GAP-associated 62 kDa protein as a docking protein, Dok. Cell 88:205-211.
    • (1997) Cell , vol.88 , pp. 205-211
    • Yamanashi, Y.1    Baltimore, D.2
  • 76
    • 0028867514 scopus 로고
    • Expression of the hepatocyte growth factor/scatter factor receptor tyrosine kinase is localized to epithelia in the adult mouse
    • Yang, X. M., and M. Park. 1995. Expression of the hepatocyte growth factor/scatter factor receptor tyrosine kinase is localized to epithelia in the adult mouse. Lab. Investig. 73:483-491.
    • (1995) Lab. Investig. , vol.73 , pp. 483-491
    • Yang, X.M.1    Park, M.2
  • 77
    • 0031171216 scopus 로고    scopus 로고
    • The IRS-signaling system during insulin and cytokine action
    • Yenush, L., and M. F. White. 1997. The IRS-signaling system during insulin and cytokine action. Bioessays 19:491-500.
    • (1997) Bioessays , vol.19 , pp. 491-500
    • Yenush, L.1    White, M.F.2
  • 78
    • 0029820085 scopus 로고    scopus 로고
    • The pleckstrin homology domain is the principle link between the insulin receptor and IRS-1
    • Yenush, L., K. J. Makati, J. Smith-Hall, O. Ishibashi, M. G. Myers, Jr., and M. F. White. 1996. The pleckstrin homology domain is the principle link between the insulin receptor and IRS-1. J. Biol. Chem. 271:24300-24306.
    • (1996) J. Biol. Chem. , vol.271 , pp. 24300-24306
    • Yenush, L.1    Makati, K.J.2    Smith-Hall, J.3    Ishibashi, O.4    Myers M.G., Jr.5    White, M.F.6
  • 79
    • 0024356856 scopus 로고
    • Purification and biological characterization of human hepatopoietin A, a polypeptide growth factor for hepatocytes
    • Zarnegar, R., and G. Michalopoulos. 1989. Purification and biological characterization of human hepatopoietin A, a polypeptide growth factor for hepatocytes. Cancer Res. 49:3314-3320.
    • (1989) Cancer Res. , vol.49 , pp. 3314-3320
    • Zarnegar, R.1    Michalopoulos, G.2
  • 81
    • 0028028202 scopus 로고
    • Tyrosine 1356 in the carboxyl-terminal tail of the HGF/SF receptor is essential for the transduction of signals for cell motility and morphogenesis
    • Zhu, H., M. A. Naujokas, E. D. Fixman, K. Torossian, and M. Park. 1994. Tyrosine 1356 in the carboxyl-terminal tail of the HGF/SF receptor is essential for the transduction of signals for cell motility and morphogenesis. J. Biol. Chem. 269:29943-29948.
    • (1994) J. Biol. Chem. , vol.269 , pp. 29943-29948
    • Zhu, H.1    Naujokas, M.A.2    Fixman, E.D.3    Torossian, K.4    Park, M.5
  • 82
    • 0028026665 scopus 로고
    • Receptor chimeras indicate that the Met tyrosine kinase mediates the motility and morphogenic responses of hepatocyte growth/scatter factor
    • Zhu, H., M. A. Naujokas, and M. Park. 1994. Receptor chimeras indicate that the Met tyrosine kinase mediates the motility and morphogenic responses of hepatocyte growth/scatter factor. Cell Growth Differ. 5:359-366.
    • (1994) Cell Growth Differ. , vol.5 , pp. 359-366
    • Zhu, H.1    Naujokas, M.A.2    Park, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.