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Volumn 118, Issue 24, 2005, Pages 5861-5871

Efficient suppression of FGF-2-induced ERK activation by the cooperative interaction among mammalian Sprouty isoforms

Author keywords

ERK pathway; FGF; Negative feedback inhibition; Receptor tyrosine kinase; Sprouty

Indexed keywords

CELL PROTEIN; FIBROBLAST GROWTH FACTOR 2; GROWTH FACTOR RECEPTOR BOUND PROTEIN 2; MITOGEN ACTIVATED PROTEIN KINASE; PROTEIN INHIBITOR; SOS PROTEIN; SPROUTY PROTEIN; SPROUTY1 PROTEIN; SPROUTY2 PROTEIN; SPROUTY3 PROTEIN; SPROUTY4 PROTEIN; UNCLASSIFIED DRUG;

EID: 30644457873     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: 10.1242/jcs.02711     Document Type: Article
Times cited : (53)

References (47)
  • 1
    • 0035902180 scopus 로고    scopus 로고
    • Oncogenic kinase signaling
    • Blume-Jensen, P. and Hunter, T. (2001). Oncogenic kinase signaling. Nature 411, 355-365.
    • (2001) Nature , vol.411 , pp. 355-365
    • Blume-Jensen, P.1    Hunter, T.2
  • 2
    • 0033970533 scopus 로고    scopus 로고
    • Dual specificity phosphatases: A gene family for control of MAP kinase function
    • Camps, M., Nichols, A. and Arkinstall, S. (1999). Dual specificity phosphatases: a gene family for control of MAP kinase function. FASEB J. 14, 6-16.
    • (1999) FASEB J. , vol.14 , pp. 6-16
    • Camps, M.1    Nichols, A.2    Arkinstall, S.3
  • 3
    • 0033525895 scopus 로고    scopus 로고
    • Sprouty, an intracellular inhibitor of Ras signaling
    • Casci, T., Vinos, J. and Freeman, M. (1999). Sprouty, an intracellular inhibitor of Ras signaling. Cell 96, 655-665.
    • (1999) Cell , vol.96 , pp. 655-665
    • Casci, T.1    Vinos, J.2    Freeman, M.3
  • 4
    • 0038057388 scopus 로고    scopus 로고
    • Split personalities: The agonistic antagonist Sprouty
    • Christofori, G. (2003). Split personalities: the agonistic antagonist Sprouty. Nat. Cell Biol. 5, 377-379.
    • (2003) Nat. Cell Biol. , vol.5 , pp. 377-379
    • Christofori, G.1
  • 5
    • 0037197922 scopus 로고    scopus 로고
    • The bimodal regulation of epidermal growth factor signaling by human Sprouty proteins
    • Egan, J. E., Hall, A. B., Yatsula, B. A. and Bar-Sagi, D. (2002). The bimodal regulation of epidermal growth factor signaling by human Sprouty proteins. Proc. Natl. Acad. Sci. USA 99, 6041-6046.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 6041-6046
    • Egan, J.E.1    Hall, A.B.2    Yatsula, B.A.3    Bar-Sagi, D.4
  • 6
    • 2042538029 scopus 로고    scopus 로고
    • Structure and regulation of MAPK phosphatases
    • Farooq, A. and Zhou, M. M. (2004). Structure and regulation of MAPK phosphatases. Cell Signal. 16, 769-779.
    • (2004) Cell Signal. , vol.16 , pp. 769-779
    • Farooq, A.1    Zhou, M.M.2
  • 7
    • 0035824694 scopus 로고    scopus 로고
    • Mammalian sprouty proteins inhibit cell growth and differentiation by preventing ras activation
    • Gross, I., Bassit, B., Benezra, M. and Licht, J. D. (2001). Mammalian sprouty proteins inhibit cell growth and differentiation by preventing ras activation. J. Biol. Chem. 276, 46460-46468.
    • (2001) J. Biol. Chem. , vol.276 , pp. 46460-46468
    • Gross, I.1    Bassit, B.2    Benezra, M.3    Licht, J.D.4
  • 8
    • 0027032705 scopus 로고
    • Mucin genes and the proteins they encode: Structure, diversity, and regulation
    • Gum, J. R. J. (1992). Mucin genes and the proteins they encode: structure, diversity, and regulation. Am. J. Respir. Cell Mol. Biol. 7, 557-564.
    • (1992) Am. J. Respir. Cell Mol. Biol. , vol.7 , pp. 557-564
    • Gum, J.R.J.1
  • 9
    • 0032559228 scopus 로고    scopus 로고
    • Sprouty encodes a novel antagonist of FGF signaling that patterns apical branching of the Drosophila airways
    • Hacohen, N., Kramer, S., Sutherland, D., Hiromi, Y. and Krasnow, M. A. (1998). sprouty encodes a novel antagonist of FGF signaling that patterns apical branching of the Drosophila airways. Cell 92, 253-263.
    • (1998) Cell , vol.92 , pp. 253-263
    • Hacohen, N.1    Kramer, S.2    Sutherland, D.3    Hiromi, Y.4    Krasnow, M.A.5
  • 10
    • 0031835659 scopus 로고    scopus 로고
    • Binding of Shp2 tyrosine phosphatase to FRS2 is essential for fibroblast growth factor-induced PC12 cell differentiation
    • Hadari, Y. R., Kouhara, H., Lax, I. and Schlessinger, J. (1998). Binding of Shp2 tyrosine phosphatase to FRS2 is essential for fibroblast growth factor-induced PC12 cell differentiation. Mol. Cell. Biol. 18, 3966-3973.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 3966-3973
    • Hadari, Y.R.1    Kouhara, H.2    Lax, I.3    Schlessinger, J.4
  • 11
    • 0037452567 scopus 로고    scopus 로고
    • hSpry2 is targeted to the ubiquitin-dependent proteasome pathway by c-Cbl
    • Hall, A. B., Jura, N., DaSilva, J., Jang, Y. J., Gong, D. and Bar-Sagi, D. (2003). hSpry2 is targeted to the ubiquitin-dependent proteasome pathway by c-Cbl. Curr. Biol. 13, 308-314.
    • (2003) Curr. Biol. , vol.13 , pp. 308-314
    • Hall, A.B.1    Jura, N.2    DaSilva, J.3    Jang, Y.J.4    Gong, D.5    Bar-Sagi, D.6
  • 12
    • 0036847930 scopus 로고    scopus 로고
    • Sprouty1 and Sprouty2 provide a control mechanism for the Ras/MAPK signaling pathway
    • Hanafusa, H., Torii, S., Yasunaga, T. and Nishida, E. (2002). Sprouty1 and Sprouty2 provide a control mechanism for the Ras/MAPK signaling pathway. Nat. Cell Biol. 4, 850-858.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 850-858
    • Hanafusa, H.1    Torii, S.2    Yasunaga, T.3    Nishida, E.4
  • 13
    • 2542433976 scopus 로고    scopus 로고
    • Shp2, an SH2-containing protein-tyrosine phosphatase, positively regulates receptor tyrosine kinase signaling by dephosphorylating and inactivating the inhibitor Sprouty
    • Hanafusa, H., Torii, S., Yasunaga, T., Matsumoto, K. and Nishida, E. (2004). Shp2, an SH2-containing protein-tyrosine phosphatase, positively regulates receptor tyrosine kinase signaling by dephosphorylating and inactivating the inhibitor Sprouty. J. Biol. Chem. 279, 22992-22995.
    • (2004) J. Biol. Chem. , vol.279 , pp. 22992-22995
    • Hanafusa, H.1    Torii, S.2    Yasunaga, T.3    Matsumoto, K.4    Nishida, E.5
  • 14
    • 0034614637 scopus 로고    scopus 로고
    • The hallmarks of cancer
    • Hanahan, D. and Weinberg, R. A. (2000). The hallmarks of cancer. Cell 100, 57-70.
    • (2000) Cell , vol.100 , pp. 57-70
    • Hanahan, D.1    Weinberg, R.A.2
  • 17
    • 0034614490 scopus 로고    scopus 로고
    • Signaling-2000 and beyond
    • Hunter, T. (2000). Signaling-2000 and beyond. Cell 100, 113-127.
    • (2000) Cell , vol.100 , pp. 113-127
    • Hunter, T.1
  • 18
    • 0035809919 scopus 로고    scopus 로고
    • Mammalian sprouty-1 and -2 are membrane-anchored phosphoprotein inhibitors of growth factor signaling in endothelial cells
    • Impagnatiello, M. A., Weitzer, S., Gannon, G., Compagni, A., Cotton, M. and Christofori, G. (2001). Mammalian sprouty-1 and -2 are membrane-anchored phosphoprotein inhibitors of growth factor signaling in endothelial cells. J. Cell Biol. 152, 1087-1098.
    • (2001) J. Cell Biol. , vol.152 , pp. 1087-1098
    • Impagnatiello, M.A.1    Weitzer, S.2    Gannon, G.3    Compagni, A.4    Cotton, M.5    Christofori, G.6
  • 19
    • 0033543653 scopus 로고    scopus 로고
    • Specific activation of the p38 mitogen-activated protein kinase signaling pathway and induction of neurite outgrowth in PC12 cells by bone morphogenetic protein-2
    • Iwasaki, S., Iguchi, M., Watanabe, K., Hoshino, R., Tsujimoto, M. and Kohno, M. (1999). Specific activation of the p38 mitogen-activated protein kinase signaling pathway and induction of neurite outgrowth in PC12 cells by bone morphogenetic protein-2. J. Biol. Chem. 274, 26503-26510.
    • (1999) J. Biol. Chem. , vol.274 , pp. 26503-26510
    • Iwasaki, S.1    Iguchi, M.2    Watanabe, K.3    Hoshino, R.4    Tsujimoto, M.5    Kohno, M.6
  • 20
    • 0013202857 scopus 로고    scopus 로고
    • Pharmacological inhibitors of the ERK signaling pathway: Application as anticancer drugs
    • Kohno, M. and Pouyssegur, J. (2003). Pharmacological inhibitors of the ERK signaling pathway: application as anticancer drugs. Prog. Cell Cycle Res. 5, 219-224.
    • (2003) Prog. Cell Cycle Res. , vol.5 , pp. 219-224
    • Kohno, M.1    Pouyssegur, J.2
  • 21
    • 0030706168 scopus 로고    scopus 로고
    • A lipid-anchored Grb2-binding protein that links FGF-receptor activation to the Ras/MAPK signaling pathway
    • Kouhara, H., Hadari, Y. R., Spivak-Kroizman, T., Schilling, J., Bar-Sagi, D., Lax, I. and Schlessinger, J. (1997). A lipid-anchored Grb2-binding protein that links FGF-receptor activation to the Ras/MAPK signaling pathway. Cell 89, 693-702.
    • (1997) Cell , vol.89 , pp. 693-702
    • Kouhara, H.1    Hadari, Y.R.2    Spivak-Kroizman, T.3    Schilling, J.4    Bar-Sagi, D.5    Lax, I.6    Schlessinger, J.7
  • 22
    • 0033035109 scopus 로고    scopus 로고
    • Sprouty: A common antagonist of FGF and EGF signaling pathways in Drosophila
    • Kramer, S., Okabe, M., Hacohen, N., Krasnow, M. A. and Hiromi, Y. (1999). Sprouty: a common antagonist of FGF and EGF signaling pathways in Drosophila. Development 126, 2515-2525.
    • (1999) Development , vol.126 , pp. 2515-2525
    • Kramer, S.1    Okabe, M.2    Hacohen, N.3    Krasnow, M.A.4    Hiromi, Y.5
  • 25
    • 0027312272 scopus 로고
    • Guanine-nucleotide-releasing factor hSos1 binds to Grb2 and links receptor tyrosine kinases to Ras signalling
    • Li, N., Batzer, A., Daly, R., Yajnik, V., Skolnik, E., Chardin, P., Bar-Sagi, D., Margolis, B. and Schlessinger, J. (1993). Guanine-nucleotide-releasing factor hSos1 binds to Grb2 and links receptor tyrosine kinases to Ras signalling. Nature 363, 85-88.
    • (1993) Nature , vol.363 , pp. 85-88
    • Li, N.1    Batzer, A.2    Daly, R.3    Yajnik, V.4    Skolnik, E.5    Chardin, P.6    Bar-Sagi, D.7    Margolis, B.8    Schlessinger, J.9
  • 26
    • 0032719944 scopus 로고    scopus 로고
    • Vertebrate Sprouty genes are induced by FGF signaling and can cause chondrodysplasia when overexpressed
    • Minowada, G., Jarvis, L. A., Chi, C. L., Neubuser, A., Sun, X., Hacohen, N., Krasnow, M. A. and Martin, G. R. (1999). Vertebrate Sprouty genes are induced by FGF signaling and can cause chondrodysplasia when overexpressed. Development 126, 4465-4475.
    • (1999) Development , vol.126 , pp. 4465-4475
    • Minowada, G.1    Jarvis, L.A.2    Chi, C.L.3    Neubuser, A.4    Sun, X.5    Hacohen, N.6    Krasnow, M.A.7    Martin, G.R.8
  • 29
    • 0032841608 scopus 로고    scopus 로고
    • Sprouty is a general inhibitor of receptor tyrosine kinase signaling
    • Reich, A., Sapir, A. and Shilo, B. (1999). Sprouty is a general inhibitor of receptor tyrosine kinase signaling. Development 126, 4139-4147.
    • (1999) Development , vol.126 , pp. 4139-4147
    • Reich, A.1    Sapir, A.2    Shilo, B.3
  • 30
    • 0027294981 scopus 로고
    • The SH2 and SH3 domains of mammalian Grb2 couple the EGF receptor to the Ras activator mSos1
    • Rozakis-Adcock, M., Fernley, R., Wade, J., Pawson, T. and Bowtell, D. (1993). The SH2 and SH3 domains of mammalian Grb2 couple the EGF receptor to the Ras activator mSos1. Nature 363, 83-85.
    • (1993) Nature , vol.363 , pp. 83-85
    • Rozakis-Adcock, M.1    Fernley, R.2    Wade, J.3    Pawson, T.4    Bowtell, D.5
  • 31
    • 0035965203 scopus 로고    scopus 로고
    • Identification of a dominant negative mutant of Sprouty that potentiates fibroblast growth factor-but not epidermal growth factor-induced ERK activation
    • Sasaki, A., Taketomi, T., Wakioka, T., Kato, R. and Yoshimura, A. (2001). Identification of a dominant negative mutant of Sprouty that potentiates fibroblast growth factor-but not epidermal growth factor-induced ERK activation. J. Biol. Chem. 276, 36804-36808.
    • (2001) J. Biol. Chem. , vol.276 , pp. 36804-36808
    • Sasaki, A.1    Taketomi, T.2    Wakioka, T.3    Kato, R.4    Yoshimura, A.5
  • 33
    • 0034644539 scopus 로고    scopus 로고
    • Cell signaling by receptor tyrosine kinase
    • Schlessinger, J. (2000). Cell signaling by receptor tyrosine kinase. Cell 103, 211-225.
    • (2000) Cell , vol.103 , pp. 211-225
    • Schlessinger, J.1
  • 34
    • 0034730323 scopus 로고    scopus 로고
    • Receptor tyrosine kinases: Specific outcomes from general signals
    • Simon, M. A. (2000). Receptor tyrosine kinases: specific outcomes from general signals. Cell 103, 13-15.
    • (2000) Cell , vol.103 , pp. 13-15
    • Simon, M.A.1
  • 35
    • 0037008732 scopus 로고    scopus 로고
    • Prolonged nuclear retention of activated extracellular signal-regulated kinase 1/2 is required for hepatocyte growth factor-induced cell motility
    • Tanimura, S., Nomura, K., Ozaki, K., Tsujimoto, M., Kondo, T. and Kohno, M. (2002). Prolonged nuclear retention of activated extracellular signal-regulated kinase 1/2 is required for hepatocyte growth factor-induced cell motility. J. Biol. Chem. 277, 28256-28264.
    • (2002) J. Biol. Chem. , vol.277 , pp. 28256-28264
    • Tanimura, S.1    Nomura, K.2    Ozaki, K.3    Tsujimoto, M.4    Kondo, T.5    Kohno, M.6
  • 36
    • 0037449202 scopus 로고    scopus 로고
    • Specific blockade of the ERK pathway inhibits the invasiveness of tumor cells: Down-regulation of matrix metalloproteinase-3/-9/-14 and CD44
    • Tanimura, S., Asato, K., Fujishiro, S. and Kohno, M. (2003). Specific blockade of the ERK pathway inhibits the invasiveness of tumor cells: down-regulation of matrix metalloproteinase-3/-9/-14 and CD44. Biochem. Biophys. Res. Commun. 304, 801-806.
    • (2003) Biochem. Biophys. Res. Commun. , vol.304 , pp. 801-806
    • Tanimura, S.1    Asato, K.2    Fujishiro, S.3    Kohno, M.4
  • 37
    • 0033602147 scopus 로고    scopus 로고
    • Conserved function of mSpry-2, a murine homolog of Drosophila sprouty, which negatively modulates respiratory organogenesis
    • Tefft, J. D., Lee, M., Smith, S., Leinwand, M., Zhao, J., Bringas, P. J., Crowe, D. L. and Warburton, D. (1999). Conserved function of mSpry-2, a murine homolog of Drosophila sprouty, which negatively modulates respiratory organogenesis. Curr. Biol. 9, 219-222.
    • (1999) Curr. Biol. , vol.9 , pp. 219-222
    • Tefft, J.D.1    Lee, M.2    Smith, S.3    Leinwand, M.4    Zhao, J.5    Bringas, P.J.6    Crowe, D.L.7    Warburton, D.8
  • 39
    • 0347417016 scopus 로고    scopus 로고
    • Signal integration during development: Insights from the Drosophila eye
    • Voas, M. G. and Rebay, I. (2004). Signal integration during development: insights from the Drosophila eye. Dev. Dyn. 229, 162-175.
    • (2004) Dev. Dyn. , vol.229 , pp. 162-175
    • Voas, M.G.1    Rebay, I.2
  • 40
    • 0033525189 scopus 로고    scopus 로고
    • Molecular determinants of oligomer formation and complement fixation in mannose-binding proteins
    • Wallis, R. and Drickamer, K. (1999). Molecular determinants of oligomer formation and complement fixation in mannose-binding proteins. J. Biol. Chem. 274, 3580-3589.
    • (1999) J. Biol. Chem. , vol.274 , pp. 3580-3589
    • Wallis, R.1    Drickamer, K.2
  • 41
    • 0033013866 scopus 로고    scopus 로고
    • Role of phosphoinositide 3-kinase in activation of ras and mitogen-activated protein kinase by epidermal growth factor
    • Wennstrom, S. and Downward, J. (1999). Role of phosphoinositide 3-kinase in activation of ras and mitogen-activated protein kinase by epidermal growth factor. Mol. Cell. Biol. 19, 4279-4288.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 4279-4288
    • Wennstrom, S.1    Downward, J.2
  • 42
    • 0035937167 scopus 로고    scopus 로고
    • Evidence for direct interaction between Sprouty and Cbl
    • Wong, E. S., Lim, J., Low, B. C., Chen, Q. and Guy, G. R. (2001). Evidence for direct interaction between Sprouty and Cbl. J. Biol. Chem. 276, 5866-5875.
    • (2001) J. Biol. Chem. , vol.276 , pp. 5866-5875
    • Wong, E.S.1    Lim, J.2    Low, B.C.3    Chen, Q.4    Guy, G.R.5
  • 43
    • 0037119950 scopus 로고    scopus 로고
    • Sprouty2 attenuates epidermal growth factor receptor ubiquitylation and endocytosis, and consequently enhances Ras/ERK signalling
    • Wong, E. S., Fong, C. W., Lim, J., Yusoff, P., Low, B. C., Langdon, W. Y. and Guy, G. R. (2002). Sprouty2 attenuates epidermal growth factor receptor ubiquitylation and endocytosis, and consequently enhances Ras/ERK signalling. EMBO J. 21, 4796-4808.
    • (2002) EMBO J. , vol.21 , pp. 4796-4808
    • Wong, E.S.1    Fong, C.W.2    Lim, J.3    Yusoff, P.4    Low, B.C.5    Langdon, W.Y.6    Guy, G.R.7
  • 44
    • 0035933734 scopus 로고    scopus 로고
    • The C terminus of sprouty is important for modulation of cellular migration and proliferation
    • Yigzaw, Y., Cartin, L., Pierre, S., Scholich, K. and Patel, T. B. (2001). The C terminus of sprouty is important for modulation of cellular migration and proliferation. J. Biol. Chem. 276, 22742-22747.
    • (2001) J. Biol. Chem. , vol.276 , pp. 22742-22747
    • Yigzaw, Y.1    Cartin, L.2    Pierre, S.3    Scholich, K.4    Patel, T.B.5
  • 45
    • 0037414772 scopus 로고    scopus 로고
    • Protein-tyrosine phosphatases-1B (PTP1B) mediates the anti-migratory actions of Sprouty
    • Yigzaw, Y., Poppleton, H. M., Sreejayan, N., Hassid, A. and Patel, T. B. (2003). Protein-tyrosine phosphatases-1B (PTP1B) mediates the anti-migratory actions of Sprouty. J. Biol. Chem. 278, 284-288.
    • (2003) J. Biol. Chem. , vol.278 , pp. 284-288
    • Yigzaw, Y.1    Poppleton, H.M.2    Sreejayan, N.3    Hassid, A.4    Patel, T.B.5
  • 47
    • 0036139884 scopus 로고    scopus 로고
    • Receptor tyrosine kinases as targets for anticancer drugs
    • Zwick, E., Bange, J. and Ullrich, A. (2002). Receptor tyrosine kinases as targets for anticancer drugs. Trends Mol. Med. 8, 17-23.
    • (2002) Trends Mol. Med. , vol.8 , pp. 17-23
    • Zwick, E.1    Bange, J.2    Ullrich, A.3


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