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Volumn 19, Issue 10, 2009, Pages 1165-1177

FGF-receptor substrate 2 functions as a molecular sensor integrating external regulatory signals into the FGF pathway

Author keywords

Co stimulation; Crosstalk; Epithelial growth factor (EGF); Fibroblast growth factor (FGF); Threonine phosphorylation

Indexed keywords

1,3 BUTADIENE DERIVATIVE; 1,4 DIAMINO 1,4 BIS(2 AMINOPHENYLTHIO) 2,3 DICYANOBUTADIENE; EPIDERMAL GROWTH FACTOR; FIBROBLAST GROWTH FACTOR; FRS2 PROTEIN, HUMAN; MEMBRANE PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; NITRILE; SIGNAL TRANSDUCING ADAPTOR PROTEIN; SMALL INTERFERING RNA;

EID: 70349776060     PISSN: 10010602     EISSN: 17487838     Source Type: Journal    
DOI: 10.1038/cr.2009.95     Document Type: Article
Times cited : (27)

References (42)
  • 1
    • 0030706168 scopus 로고    scopus 로고
    • A lipid-an- chored Grb2-binding protein that links FGF-receptor activation to the Ras/MAPK signaling pathway
    • Kouhara H, Hadari YR, Spivak-Kroizman T, et al. A lipid-an- chored Grb2-binding protein that links FGF-receptor activation to the Ras/MAPK signaling pathway. Cell 1997; 89:693-702.
    • (1997) Cell , vol.89 , pp. 693-702
    • Kouhara, H.1    Hadari, Y.R.2    Spivak-Kroizman, T.3
  • 2
    • 0035902581 scopus 로고    scopus 로고
    • Critical role for the docking-protein FRS2 alpha in FGF receptor-mediated signal transduction pathways
    • Hadari YR, Gotoh N, Kouhara H, et al. Critical role for the docking-protein FRS2 alpha in FGF receptor-mediated signal transduction pathways. Proc Natl Acad Sci USA 2001; 98:8578-8583.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 8578-8583
    • Hadari, Y.R.1    Gotoh, N.2    Kouhara, H.3
  • 3
    • 0031835659 scopus 로고    scopus 로고
    • Binding of Shp2 tyro- sine phosphatase to FRS2 is essential for fibroblast growth factor-induced PC12 cell differentiation
    • Hadari YR, Kouhara H, Lax I, et al. Binding of Shp2 tyro- sine phosphatase to FRS2 is essential for fibroblast growth factor-induced PC12 cell differentiation. Mol Cell Biol 1998; 18:3966-3973.
    • (1998) Mol Cell Biol , vol.18 , pp. 3966-3973
    • Hadari, Y.R.1    Kouhara, H.2    Lax, I.3
  • 4
    • 0033974109 scopus 로고    scopus 로고
    • FRS2 proteins recruit intracellular signaling pathways by binding to diverse targets on fibroblast growth factor and nerve growth factor receptors
    • Ong SH, Guy GR, Hadari YR, et al. FRS2 proteins recruit intracellular signaling pathways by binding to diverse targets on fibroblast growth factor and nerve growth factor receptors. Mol Cell Biol 2000; 20:979-989.
    • (2000) Mol Cell Biol , vol.20 , pp. 979-989
    • Ong, S.H.1    Guy, G.R.2    Hadari, Y.R.3
  • 5
    • 0029764511 scopus 로고    scopus 로고
    • Broadly expressed SNT-like proteins link FGF receptor stimulation to activators of Ras
    • Wang JK, Xu H, Li HC, et al. Broadly expressed SNT-like proteins link FGF receptor stimulation to activators of Ras. Oncogene 1996; 13:721-729.
    • (1996) Oncogene , vol.13 , pp. 721-729
    • Wang, J.K.1    Xu, H.2    Li, H.C.3
  • 6
    • 0032540941 scopus 로고    scopus 로고
    • Novel recognition motif on fibroblast growth factor receptor mediates direct association and activation of SNT adapter proteins
    • Xu H, Lee KW and Goldfarb M. Novel recognition motif on fibroblast growth factor receptor mediates direct association and activation of SNT adapter proteins. J Biol Chem 1998; 273:17987-17990.
    • (1998) J Biol Chem , vol.273 , pp. 17987-17990
    • Xu, H.1    Lee, K.W.2    Goldfarb, M.3
  • 7
    • 0035933094 scopus 로고    scopus 로고
    • Stimulation of phos- phatidylinositol 3-kinase by fibroblast growth factor receptors is mediated by coordinated recruitment of multiple docking proteins
    • Ong SH, Hadari YR, Gotoh N, et al. Stimulation of phos- phatidylinositol 3-kinase by fibroblast growth factor receptors is mediated by coordinated recruitment of multiple docking proteins. Proc Natl Acad Sci USA 2001; 98:6074-6079.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 6074-6079
    • Ong, S.H.1    Hadari, Y.R.2    Gotoh, N.3
  • 8
    • 0034967978 scopus 로고    scopus 로고
    • Docking protein FRS2 links the protein tyrosine kinase RET and its oncogenic forms with the mitogen-activated protein kinase signaling cascade
    • Melillo RM, Santoro M, Ong SH, et al. Docking protein FRS2 links the protein tyrosine kinase RET and its oncogenic forms with the mitogen-activated protein kinase signaling cascade. Mol Cell Biol 2001; 21:4177-4187.
    • (2001) Mol Cell Biol , vol.21 , pp. 4177-4187
    • Melillo, R.M.1    Santoro, M.2    Ong, S.H.3
  • 9
    • 0037053398 scopus 로고    scopus 로고
    • FRS2 PTB domain conformation regulates interactions with divergent neurotrophic receptors
    • Yan KS, Kuti M, Yan S, et al. FRS2 PTB domain conformation regulates interactions with divergent neurotrophic receptors. J Biol Chem 2002; 277:17088-17094.
    • (2002) J Biol Chem , vol.277 , pp. 17088-17094
    • Yan, K.S.1    Kuti, M.2    Yan, S.3
  • 10
    • 0036672917 scopus 로고    scopus 로고
    • Fibroblast growth factor receptor substrate 2 participates in vascular endothelial growth factor-induced signaling
    • Stoletov KV, Ratcliffe KE, Terman BI. Fibroblast growth factor receptor substrate 2 participates in vascular endothelial growth factor-induced signaling. FASEB J 2002; 16:1283-1285.
    • (2002) FASEB J , vol.16 , pp. 1283-1285
    • Stoletov, K.V.1    Ratcliffe, K.E.2    Terman, B.I.3
  • 11
    • 0033635195 scopus 로고    scopus 로고
    • Structural basis of SNT PTB domain interactions with distinct neurotrophic receptors
    • Dhalluin C, Yan KS, Plotnikova O, et al. Structural basis of SNT PTB domain interactions with distinct neurotrophic receptors. Mol Cell 2000; 6:921-929.
    • (2000) Mol Cell , vol.6 , pp. 921-929
    • Dhalluin, C.1    Yan, K.S.2    Plotnikova, O.3
  • 12
    • 0037076329 scopus 로고    scopus 로고
    • FRS2 alpha attenuates FGF receptor signaling by Grb2-mediated recruitment of the ubiquitin ligase Cbl
    • Wong A, Lamothe B, Lee A, et al. FRS2 alpha attenuates FGF receptor signaling by Grb2-mediated recruitment of the ubiquitin ligase Cbl. Proc Natl Acad Sci USA 2002; 99:6684-6689.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 6684-6689
    • Wong, A.1    Lamothe, B.2    Lee, A.3
  • 14
    • 0036771763 scopus 로고    scopus 로고
    • The docking protein FRS- 2alpha controls a MAP kinase-mediated negative feedback mechanism for signaling by FGF receptors
    • Lax I, Wong A, Lamothe B, et al. The docking protein FRS- 2alpha controls a MAP kinase-mediated negative feedback mechanism for signaling by FGF receptors. Mol Cell 2002; 10:709-719.
    • (2002) Mol Cell , vol.10 , pp. 709-719
    • Lax, I.1    Wong, A.2    Lamothe, B.3
  • 15
    • 0141738653 scopus 로고    scopus 로고
    • EGFR and FGFR signaling through FRS2 is subject to negative feedback control by ERK1/2
    • Wu Y, Chen Z, Ullrich A. EGFR and FGFR signaling through FRS2 is subject to negative feedback control by ERK1/2. Biol Chem 2003; 384:1215-1226.
    • (2003) Biol Chem , vol.384 , pp. 1215-1226
    • Wu, Y.1    Chen, Z.2    Ullrich, A.3
  • 16
    • 0034636685 scopus 로고    scopus 로고
    • Regulation of mitogen-activated protein kinase signaling networks by G protein-coupled receptors
    • 2000:RE1
    • Gutkind JS. Regulation of mitogen-activated protein kinase signaling networks by G protein-coupled receptors. Sci STKE 2000; 2000:RE1.
    • (2000) Nature , vol.2001 , Issue.410 , pp. 37-40
    • Gutkind, J.S.1
  • 17
    • 0035282334 scopus 로고    scopus 로고
    • Mammalian MAP kinase signalling cascades
    • Chang L, Karin M. Mammalian MAP kinase signalling cascades. Nature 2001; 410:37-40.
    • (2001) Nature , vol.410 , pp. 37-40
    • Chang, L.1    Karin, M.2
  • 18
    • 0037810249 scopus 로고    scopus 로고
    • Signal transduction mediated by the Ras/Raf/MEK/ERK pathway from cytokine receptors to transcription factors: Potential targeting for therapeutic intervention
    • Chang F, Steelman LS, Lee JT, et al. Signal transduction mediated by the Ras/Raf/MEK/ERK pathway from cytokine receptors to transcription factors: potential targeting for therapeutic intervention. Leukemia 2003; 17:1263-1293.
    • (2003) Leukemia , vol.17 , pp. 1263-1293
    • Chang, F.1    Steelman, L.S.2    Lee, J.T.3
  • 19
    • 0033593404 scopus 로고    scopus 로고
    • Morphogenesis
    • Hogan BL. Morphogenesis. Cell 1999; 96:225-233.
    • (1999) Cell , vol.96 , pp. 225-233
    • Hogan, B.L.1
  • 20
    • 0033032591 scopus 로고    scopus 로고
    • Signaling networks--do all roads lead to the same genes?
    • Pawson T, Saxton TM. Signaling networks--do all roads lead to the same genes? Cell 1999; 97:675-678.
    • (1999) Cell , vol.97 , pp. 675-678
    • Pawson, T.1    Saxton, T.M.2
  • 21
    • 0034644539 scopus 로고    scopus 로고
    • Cell signaling by receptor tyrosine kinases
    • Schlessinger J. Cell signaling by receptor tyrosine kinases. Cell 2000; 103:211-225.
    • (2000) Cell , vol.103 , pp. 211-225
    • Schlessinger, J.1
  • 22
    • 0037205044 scopus 로고    scopus 로고
    • Signaling pathways for PC12 cell differentiation: Making the right connections
    • Vaudry D, Stork PJ, Lazarovici P, et al. Signaling pathways for PC12 cell differentiation: making the right connections. Science 2002; 296:1648-1649.
    • (2002) Science , vol.296 , pp. 1648-1649
    • Vaudry, D.1    Stork, P.J.2    Lazarovici, P.3
  • 23
    • 0029011218 scopus 로고
    • The MAPK signaling cascade
    • Seger R, Krebs EG. The MAPK signaling cascade. FASEB J 1995; 9:726-735.
    • (1995) FASEB J , vol.9 , pp. 726-735
    • Seger, R.1    Krebs, E.G.2
  • 24
    • 0025888298 scopus 로고
    • Identification of substrate recognition determinants for human ERK1 and ERK2 protein kinases
    • Gonzalez FA, Raden DL, Davis RJ. Identification of substrate recognition determinants for human ERK1 and ERK2 protein kinases. J Biol Chem 1991; 266:22159-22163.
    • (1991) J Biol Chem , vol.266 , pp. 22159-22163
    • Gonzalez, F.A.1    Raden, D.L.2    Davis, R.J.3
  • 25
    • 0033555229 scopus 로고    scopus 로고
    • Multiple docking sites on substrate proteins form a modular system that mediates recognition by ERK MAP kinase
    • Jacobs D, Glossip D, Xing H, et al. Multiple docking sites on substrate proteins form a modular system that mediates recognition by ERK MAP kinase. Genes Dev 1999; 13:163-175.
    • (1999) Genes Dev , vol.13 , pp. 163-175
    • Jacobs, D.1    Glossip, D.2    Xing, H.3
  • 26
    • 0033788484 scopus 로고    scopus 로고
    • A conserved docking motif in MAP kinases common to substrates, activators and regulators
    • Tanoue T, Adachi M, Moriguchi T, et al. A conserved docking motif in MAP kinases common to substrates, activators and regulators. Nat Cell Biol 2000; 2:110-116.
    • (2000) Nat Cell Biol , vol.2 , pp. 110-116
    • Tanoue, T.1    Adachi, M.2    Moriguchi, T.3
  • 27
    • 0035920179 scopus 로고    scopus 로고
    • Docking sites on substrate proteins direct extracellular signal-regulated ki- nase to phosphorylate specific residues
    • Fantz DA, Jacobs D, Glossip D, et al. Docking sites on substrate proteins direct extracellular signal-regulated ki- nase to phosphorylate specific residues. J Biol Chem 2001; 276:27256-27265.
    • (2001) J Biol Chem , vol.276 , pp. 27256-27265
    • Fantz, D.A.1    Jacobs, D.2    Glossip, D.3
  • 28
    • 0027395119 scopus 로고
    • Kaplan DR. SNT, a differentiation- specific target of neurotrophic factor-induced tyrosine kinase activity in neurons and PC12 cells
    • Rabin SJ, Cleghon V, Kaplan DR. SNT, a differentiation- specific target of neurotrophic factor-induced tyrosine kinase activity in neurons and PC12 cells. Mol Cell Biol 1993; 13:2203-2213.
    • (1993) Mol Cell Biol , vol.13 , pp. 2203-2213
    • Rabin, S.J.1    Cleghon, V.2
  • 29
    • 5444246276 scopus 로고    scopus 로고
    • SNT-2 interacts with ERK2 and negatively regulates ERK2 signaling in response to EGF stimulation
    • Huang L, Gotoh N, Zhang S, et al. SNT-2 interacts with ERK2 and negatively regulates ERK2 signaling in response to EGF stimulation. Biochem Biophys Res Commun 2004; 324:1011-1017.
    • (2004) Biochem Biophys Res Commun , vol.324 , pp. 1011-1017
    • Huang, L.1    Gotoh, N.2    Zhang, S.3
  • 30
    • 33750214274 scopus 로고    scopus 로고
    • Unique role of SNT-2/FRS2beta/FRS3 docking/adaptor protein for negative regulation in EGF receptor tyrosine kinase signaling pathways
    • Huang L, Watanabe M, Chikamori M, et al. Unique role of SNT-2/FRS2beta/FRS3 docking/adaptor protein for negative regulation in EGF receptor tyrosine kinase signaling pathways. Oncogene 2006; 25:6457-6466.
    • (2006) Oncogene , vol.25 , pp. 6457-6466
    • Huang, L.1    Watanabe, M.2    Chikamori, M.3
  • 31
    • 0035254671 scopus 로고    scopus 로고
    • Identification of a docking groove on ERK and p38 MAP kinases that regulates the specificity of docking interactions
    • Tanoue T, Maeda R, Adachi M, et al. Identification of a docking groove on ERK and p38 MAP kinases that regulates the specificity of docking interactions. EMBO J 2001; 20:466-479.
    • (2001) EMBO J , vol.20 , pp. 466-479
    • Tanoue, T.1    Maeda, R.2    Adachi, M.3
  • 32
    • 33744798469 scopus 로고    scopus 로고
    • Docking interactions induce exposure of activation loop in the MAP kinase ERK2
    • Zhou T, Sun L, Humphreys J, et al. Docking interactions induce exposure of activation loop in the MAP kinase ERK2. Structure 2006; 14:1011-1019.
    • (2006) Structure , vol.14 , pp. 1011-1019
    • Zhou, T.1    Sun, L.2    Humphreys, J.3
  • 33
    • 0030061922 scopus 로고    scopus 로고
    • IRS-1-mediated inhibition of insulin receptor tyrosine kinase activity in TNF- alpha- and obesity-induced insulin resistance
    • Hotamisligil GS, Peraldi P, Budavari A, et al. IRS-1-mediated inhibition of insulin receptor tyrosine kinase activity in TNF- alpha- and obesity-induced insulin resistance. Science 1996; 271:665-668.
    • (1996) Science , vol.271 , pp. 665-668
    • Hotamisligil, G.S.1    Peraldi, P.2    Budavari, A.3
  • 34
    • 0030015109 scopus 로고    scopus 로고
    • Different effects of insulin and platelet-derived growth factor on phos- phatidylinositol 3-kinase at the subcellular level in 3T3-L1 adipocytes. A possible explanation for their specific effects on glucose transport
    • Ricort JM, Tanti JF, Van Obberghen E, et al. Different effects of insulin and platelet-derived growth factor on phos- phatidylinositol 3-kinase at the subcellular level in 3T3-L1 adipocytes. A possible explanation for their specific effects on glucose transport. Eur JBiochem 1996; 239:17-22.
    • (1996) Eur JBiochem , vol.239 , pp. 17-22
    • Ricort, J.M.1    Tanti, J.F.2    Van Obberghen, E.3
  • 35
    • 0037339991 scopus 로고    scopus 로고
    • Three mitogen- activated protein kinases inhibit insulin signaling by different mechanisms in 3T3-L1 adipocytes
    • Fujishiro M, Gotoh Y, Katagiri H, et al. Three mitogen- activated protein kinases inhibit insulin signaling by different mechanisms in 3T3-L1 adipocytes. Mol Endocrinol 2003; 17:487-497.
    • (2003) Mol Endocrinol , vol.17 , pp. 487-497
    • Fujishiro, M.1    Gotoh, Y.2    Katagiri, H.3
  • 36
    • 0035947724 scopus 로고    scopus 로고
    • Identification of the mechanisms regulating the differential activation of the mapk cascade by epidermal growth factor and nerve growth factor in PC12 cells
    • Kao S, Jaiswal RK, Kolch W, et al. Identification of the mechanisms regulating the differential activation of the mapk cascade by epidermal growth factor and nerve growth factor in PC12 cells. J Biol Chem 2001; 276:18169-18177.
    • (2001) J Biol Chem , vol.276 , pp. 18169-18177
    • Kao, S.1    Jaiswal, R.K.2    Kolch, W.3
  • 37
    • 0022137480 scopus 로고
    • Microinjection of the ras oncogene protein into PC12 cells induces morphological differentiation
    • Bar-Sagi D, Feramisco JR. Microinjection of the ras oncogene protein into PC12 cells induces morphological differentiation. Cell 1985; 42:841-848.
    • (1985) Cell , vol.42 , pp. 841-848
    • Bar-Sagi, D.1    Feramisco, J.R.2
  • 38
    • 0022347122 scopus 로고
    • Sarcoma viruses carrying ras oncogenes induce differentiation-associated properties in a neuronal cell line
    • Noda M, Ko M, Ogura A, et al. Sarcoma viruses carrying ras oncogenes induce differentiation-associated properties in a neuronal cell line. Nature 1985; 318:73-75.
    • (1985) Nature , vol.318 , pp. 73-75
    • Noda, M.1    Ko, M.2    Ogura, A.3
  • 39
    • 0141742631 scopus 로고    scopus 로고
    • Fibroblast growth factors and their receptors in the central nervous system
    • Reuss B, von Bohlen und Halbach O. Fibroblast growth factors and their receptors in the central nervous system. Cell Tissue Res 2003; 313:139-157.
    • (2003) Cell Tissue Res , vol.313 , pp. 139-157
    • Von Bohlen, R.B.1    Halbach, O.2
  • 40
    • 33645068866 scopus 로고    scopus 로고
    • Context-specific requirements for Fgfr1 signaling through Frs2 and Frs3 during mouse development
    • Hoch RV, Soriano P. Context-specific requirements for Fgfr1 signaling through Frs2 and Frs3 during mouse development. Development 2006; 133:663-673.
    • (2006) Development , vol.133 , pp. 663-673
    • Hoch, R.V.1    Soriano, P.2
  • 41
    • 11244251791 scopus 로고    scopus 로고
    • Direct cell cycle regulation by the fibroblast growth factor receptor (FGFR) kinase through phosphorylation-dependent release of Cks1 from FGFR substrate 2
    • Zhang Y, Lin Y, Bowles C, et al. Direct cell cycle regulation by the fibroblast growth factor receptor (FGFR) kinase through phosphorylation- dependent release of Cks1 from FGFR substrate 2. J Biol Chem 2004; 279:55348-55354.
    • (2004) J Biol Chem , vol.279 , pp. 55348-55354
    • Zhang, Y.1    Lin, Y.2    Bowles, C.3
  • 42
    • 24044544231 scopus 로고    scopus 로고
    • Direct interaction of Rnd1 with FRS2 beta regulates Rnd1-induced down-regulation of RhoA activity and is involved in fibroblast growth factor- induced neurite outgrowth in PC12 cells
    • Harada A, Katoh H, Negishi M. Direct interaction of Rnd1 with FRS2 beta regulates Rnd1-induced down-regulation of RhoA activity and is involved in fibroblast growth factor- induced neurite outgrowth in PC12 cells. J Biol Chem 2005; 280:18418-18424.
    • (2005) J Biol Chem , vol.280 , pp. 18418-18424
    • Harada, A.1    Katoh, H.2    Negishi, M.3


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