메뉴 건너뛰기
Journal of Cell Biology
Volumn 200, Issue 4, 2013, Pages 493-504
Grb2 controls phosphorylation of FGFR2 by inhibiting receptor kinase and Shp2 phosphatase activity
Author keywords

[No Author keywords available]
Indexed keywords

EPIDERMAL GROWTH FACTOR RECEPTOR; FIBROBLAST GROWTH FACTOR RECEPTOR 2; GROWTH FACTOR RECEPTOR BOUND PROTEIN 2; PROTEIN TYROSINE PHOSPHATASE SHP 2;
EID: 84874368710     PISSN: 00219525     EISSN: 15408140     Source Type: Journal    
DOI: 10.1083/jcb.201204106     Document Type: Article
Times cited : (58)
References (44)
  • 1
    • 0038190924 scopus 로고    scopus 로고
    • Development of an efficient "substratetrapping" mutant of Src homology phosphotyrosine phosphatase 2 and identification of the epidermal growth factor receptor, Gab1, and three other proteins as target substrates
    • Agazie, Y.M., and M.J. Hayman. 2003. Development of an efficient "substratetrapping" mutant of Src homology phosphotyrosine phosphatase 2 and identification of the epidermal growth factor receptor, Gab1, and three other proteins as target substrates. J. Biol. Chem. 278:13952-13958. http://dx.doi.org/10.1074/jbc.M210670200
    • (2003) J. Biol. Chem. , vol.278 , pp. 13952-13958
    • Agazie, Y.M.1    Hayman, M.J.2
  • 2
    • 46249129455 scopus 로고    scopus 로고
    • Extracellular point mutations in FGFR2 elicit unexpected changes in intracellular signalling
    • Ahmed, Z., A.C. Schüller, K. Suhling, C. Tregidgo, and J.E. Ladbury. 2008. Extracellular point mutations in FGFR2 elicit unexpected changes in intracellular signalling. Biochem. J. 413:37-49. http://dx.doi.org/10.1042/BJ20071594
    • (2008) Biochem. J. , vol.413 , pp. 37-49
    • Ahmed, Z.1    Schüller, A.C.2    Suhling, K.3    Tregidgo, C.4    Ladbury, J.E.5
  • 3
  • 4
    • 0142211311 scopus 로고    scopus 로고
    • Tyrosyl phosphorylation of Shp2 is required for normal ERK activation in response to some, but not all, growth factors
    • Araki, T., H. Nawa, and B.G. Neel. 2003. Tyrosyl phosphorylation of Shp2 is required for normal ERK activation in response to some, but not all, growth factors. J. Biol. Chem. 278:41677-41684. http://dx.doi.org/10.1074/jbc.M306461200
    • (2003) J. Biol. Chem. , vol.278 , pp. 41677-41684
    • Araki, T.1    Nawa, H.2    Neel, B.G.3
  • 5
    • 0032521428 scopus 로고    scopus 로고
    • Revealing mechanisms for SH2 domain mediated regulation of the protein tyrosine phosphatase SHP-2
    • Barford, D., and B.G. Neel. 1998. Revealing mechanisms for SH2 domain mediated regulation of the protein tyrosine phosphatase SHP-2. Structure. 6:249-254. http://dx.doi.org/10.1016/S0969-2126(98)00027-6
    • (1998) Structure. , vol.6 , pp. 249-254
    • Barford, D.1    Neel, B.G.2
  • 6
    • 10644268691 scopus 로고    scopus 로고
    • Substrate-trapping techniques in the identification of cellular PTP targets
    • Blanchetot, C., M. Chagnon, N. Dubé, M. Hallé, and M.L. Tremblay. 2005. Substrate-trapping techniques in the identification of cellular PTP targets. Methods. 35:44-53. http://dx.doi.org/10.1016/j.ymeth.2004.07.007
    • (2005) Methods. , vol.35 , pp. 44-53
    • Blanchetot, C.1    Chagnon, M.2    Dubé, N.3    Hallé, M.4    Tremblay, M.L.5
  • 8
    • 40949090037 scopus 로고    scopus 로고
    • Involvement of fibroblast growth factor receptor 2 isoform switching in mammary oncogenesis
    • Cha, J.Y., Q.T. Lambert, G.W. Reuther, and C.J. Der. 2008. Involvement of fibroblast growth factor receptor 2 isoform switching in mammary oncogenesis. Mol. Cancer Res. 6:435-445. http://dx.doi.org/10.1158/1541-7786.MCR-07-0187
    • (2008) Mol. Cancer Res. , vol.6 , pp. 435-445
    • Cha, J.Y.1    Lambert, Q.T.2    Reuther, G.W.3    Der, C.J.4
  • 9
    • 65249140043 scopus 로고    scopus 로고
    • Aberrant receptor internalization and enhanced FRS2-dependent signaling contribute to the transforming activity of the fibroblast growth factor receptor 2 IIIb C3 isoform
    • Cha, J.Y., S. Maddileti, N. Mitin, T.K. Harden, and C.J. Der. 2009. Aberrant receptor internalization and enhanced FRS2-dependent signaling contribute to the transforming activity of the fibroblast growth factor receptor 2 IIIb C3 isoform. J. Biol. Chem. 284:6227-6240. http://dx.doi.org/10.1074/jbc.M803998200
    • (2009) J. Biol. Chem. , vol.284 , pp. 6227-6240
    • Cha, J.Y.1    Maddileti, S.2    Mitin, N.3    Harden, T.K.4    Der, C.J.5
  • 13
    • 0027531637 scopus 로고
    • SH2-containing phosphotyrosine phosphatase as a target of protein-tyrosine kinases
    • Feng, G.S., C.C. Hui, and T. Pawson. 1993. SH2-containing phosphotyrosine phosphatase as a target of protein-tyrosine kinases. Science. 259:1607-1611. http://dx.doi.org/10.1126/science.8096088
    • (1993) Science. , vol.259 , pp. 1607-1611
    • Feng, G.S.1    Hui, C.C.2    Pawson, T.3
  • 14
    • 0026471539 scopus 로고
    • Identification of a human src homology 2-containing protein-tyrosine-phosphatase: a putative homolog of Drosophila corkscrew
    • Freeman, R.M. Jr., J. Plutzky, and B.G. Neel. 1992. Identification of a human src homology 2-containing protein-tyrosine-phosphatase: a putative homolog of Drosophila corkscrew. Proc. Natl. Acad. Sci. USA. 89:11239-11243. http://dx.doi.org/10.1073/pnas.89.23.11239
    • (1992) Proc. Natl. Acad. Sci. USA. , vol.89 , pp. 11239-11243
    • Freeman Jr., R.M.1    Plutzky, J.2    Neel, B.G.3
  • 15
    • 0141885098 scopus 로고    scopus 로고
    • Conditional activation of fibroblast growth factor receptor (FGFR) 1, but not FGFR2, in prostate cancer cells leads to increased osteopontin induction, extracellular signal-regulated kinase activation, and in vivo proliferation
    • Freeman, K.W., R.D. Gangula, B.E. Welm, M. Ozen, B.A. Foster, J.M. Rosen, M. Ittmann, N.M. Greenberg, and D.M. Spencer. 2003. Conditional activation of fibroblast growth factor receptor (FGFR) 1, but not FGFR2, in prostate cancer cells leads to increased osteopontin induction, extracellular signal-regulated kinase activation, and in vivo proliferation. Cancer Res. 63:6237-6243.
    • (2003) Cancer Res. , vol.63 , pp. 6237-6243
    • Freeman, K.W.1    Gangula, R.D.2    Welm, B.E.3    Ozen, M.4    Foster, B.A.5    Rosen, J.M.6    Ittmann, M.7    Greenberg, N.M.8    Spencer, D.M.9
  • 17
    • 77955293912 scopus 로고    scopus 로고
    • Germline and somatic mosaicism for FGFR2 mutation in the mother of a child with Crouzon syndrome: Implications for genetic testing in "paternal age-effect" syndromes
    • Goriely, A., H. Lord, J. Lim, D. Johnson, T. Lester, H.V. Firth, and A.O. Wilkie. 2010. Germline and somatic mosaicism for FGFR2 mutation in the mother of a child with Crouzon syndrome: Implications for genetic testing in "paternal age-effect" syndromes. Am. J. Med. Genet. A. 152A:2067-2073. http://dx.doi.org/10.1002/ajmg.a.33513
    • (2010) Am. J. Med. Genet. A. , vol.152 A , pp. 2067-2073
    • Goriely, A.1    Lord, H.2    Lim, J.3    Johnson, D.4    Lester, T.5    Firth, H.V.6    Wilkie, A.O.7
  • 18
    • 77954638588 scopus 로고    scopus 로고
    • The tyrosine phosphatase Shp2 in development and cancer
    • Grossmann, K.S., M. Rosário, C. Birchmeier, and W. Birchmeier. 2010. The tyrosine phosphatase Shp2 in development and cancer. Adv. Cancer Res. 196:53-89. http://dx.doi.org/10.1016/S0065-230X(10)06002-1
    • (2010) Adv. Cancer Res. , vol.106 , pp. 53-89
    • Grossmann, K.S.1    Rosário, M.2    Birchmeier, C.3    Birchmeier, W.4
  • 19
    • 0031835659 scopus 로고    scopus 로고
    • Binding of Shp2 tyrosine phosphatase to FRS2 is essential for fibroblast growth factorinduced PC12 cell differentiation
    • Hadari, Y.R., H. Kouhara, I. Lax, and J. Schlessinger. 1998. Binding of Shp2 tyrosine phosphatase to FRS2 is essential for fibroblast growth factorinduced 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
  • 22
    • 0032548830 scopus 로고    scopus 로고
    • Crystal structure of the tyrosine phosphatase SHP-2
    • Hof, P., S. Pluskey, S. Dhe-Paganon, M.J. Eck, and S.E. Shoelson. 1998. Crystal structure of the tyrosine phosphatase SHP-2. Cell. 92:441-450. http://dx.doi.org/10.1016/S0092-8674(00)80938-1
    • (1998) Cell. , vol.92 , pp. 441-450
    • Hof, P.1    Pluskey, S.2    Dhe-Paganon, S.3    Eck, M.J.4    Shoelson, S.E.5
  • 23
    • 0030028790 scopus 로고    scopus 로고
    • A Grb2-associated docking protein in EGF-and insulinreceptor signalling
    • 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 insulinreceptor signalling. Nature. 379:560-564. http://dx.doi.org/10.1038/379560a0
    • (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
  • 24
    • 0029012406 scopus 로고
    • A truncated K-sam product lacking the distal carboxyl-terminal portion provides a reduced level of autophosphorylation and greater resistance against induction of differentiation
    • Ishii, H., T. Yoshida, H. Oh, S. Yoshida, and M. Terada. 1995. A truncated K-sam product lacking the distal carboxyl-terminal portion provides a reduced level of autophosphorylation and greater resistance against induction of differentiation. Mol. Cell. Biol. 15:3664-3671.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 3664-3671
    • Ishii, H.1    Yoshida, T.2    Oh, H.3    Yoshida, S.4    Terada, M.5
  • 26
    • 0035328856 scopus 로고    scopus 로고
    • Mutations in fibroblast growth factor receptor 2 and fibroblast growth factor receptor 3 genes associated with human gastric and colorectal cancers
    • Jang, J.H., K.H. Shin, and J.G. Park. 2001. Mutations in fibroblast growth factor receptor 2 and fibroblast growth factor receptor 3 genes associated with human gastric and colorectal cancers. Cancer Res. 61:3541-3543.
    • (2001) Cancer Res. , vol.61 , pp. 3541-3543
    • Jang, J.H.1    Shin, K.H.2    Park, J.G.3
  • 27
    • 0033870788 scopus 로고    scopus 로고
    • A novel mutation, Ala315Ser, in FGFR2: a gene-environment interaction leading to craniosynostosis?
    • Johnson, D., S.A. Wall, S. Mann, and A.O. Wilkie. 2000. A novel mutation, Ala315Ser, in FGFR2: a gene-environment interaction leading to craniosynostosis? Eur. J. Hum. Genet. 8:571-577. http://dx.doi.org/10.1038/sj.ejhg.5200499
    • (2000) Eur. J. Hum. Genet. , vol.8 , pp. 571-577
    • Johnson, D.1    Wall, S.A.2    Mann, S.3    Wilkie, A.O.4
  • 29
    • 80052211582 scopus 로고    scopus 로고
    • Rapid phospho-turnover by receptor tyrosine kinases impacts downstream signaling and drug binding
    • Kleiman, L.B., T. Maiwald, H. Conzelmann, D.A. Lauffenburger, and P.K. Sorger. 2011. Rapid phospho-turnover by receptor tyrosine kinases impacts downstream signaling and drug binding. Mol. Cell. 43:723-737. http://dx.doi.org/10.1016/j.molcel.2011.07.014
    • (2011) Mol. Cell. , vol.43 , pp. 723-737
    • Kleiman, L.B.1    Maiwald, T.2    Conzelmann, H.3    Lauffenburger, D.A.4    Sorger, P.K.5
  • 30
    • 0033965233 scopus 로고    scopus 로고
    • Basic fibroblast growth factor confers a less malignant phenotype in MDA-MB-231 human breast cancer cells
    • Korah, R.M., V. Sysounthone, Y. Golowa, and R. Wieder. 2000. Basic fibroblast growth factor confers a less malignant phenotype in MDA-MB-231 human breast cancer cells. Cancer Res. 60:733-740.
    • (2000) Cancer Res. , vol.60 , pp. 733-740
    • Korah, R.M.1    Sysounthone, V.2    Golowa, Y.3    Wieder, R.4
  • 31
    • 0030706168 scopus 로고    scopus 로고
    • A lipid-anchored Grb2-binding protein that links FGF-receptor activation to the Ras/MAPK signaling pathway
    • Kouhara, H., Y.R. Hadari, T. Spivak-Kroizman, J. Schilling, D. Bar-Sagi, I. Lax, and J. Schlessinger. 1997. A lipid-anchored Grb2-binding protein that links FGF-receptor activation to the Ras/MAPK signaling pathway. Cell. 89:693-702. http://dx.doi.org/10.1016/S0092-8674(00)80252-4
    • (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
  • 34
    • 0034758469 scopus 로고    scopus 로고
    • Site-specific incorporation of a phosphotyrosine mimetic reveals a role for tyrosine phosphorylation of SHP-2 in cell signaling
    • Lu, W., D. Gong, D. Bar-Sagi, and P.A. Cole. 2001. Site-specific incorporation of a phosphotyrosine mimetic reveals a role for tyrosine phosphorylation of SHP-2 in cell signaling. Mol. Cell. 8:759-769. http://dx.doi.org/10.1016/S1097-2765(01)00369-0
    • (2001) Mol. Cell. , vol.8 , pp. 759-769
    • Lu, W.1    Gong, D.2    Bar-Sagi, D.3    Cole, P.A.4
  • 35
    • 79956039791 scopus 로고    scopus 로고
    • SH2 domain-containing proteintyrosine phosphatases
    • Neel, B.G., G. Chan, and S. Dhanji. 2010. SH2 domain-containing proteintyrosine phosphatases. Handbook of Cell Signaling 2:771-809.
    • (2010) Handbook of Cell Signaling , vol.2 , pp. 771-809
    • Neel, B.G.1    Chan, G.2    Dhanji, S.3
  • 36
    • 0037665155 scopus 로고    scopus 로고
    • Specificity is complex and time consuming: mutual exclusivity in tyrosine kinase-mediated signaling
    • O'Rourke, L., and J.E. Ladbury. 2003. Specificity is complex and time consuming: mutual exclusivity in tyrosine kinase-mediated signaling. Acc. Chem. Res. 36:410-416. http://dx.doi.org/10.1021/ar020167s
    • (2003) Acc. Chem. Res. , vol.36 , pp. 410-416
    • O'Rourke, L.1    Ladbury, J.E.2
  • 38
    • 0027294981 scopus 로고
    • The SH2 and SH3 domains of mammalian Grb2 couple the EGF receptor to the Ras activator mSos1
    • Rozakis-Adcock, M., R. Fernley, J. Wade, T. Pawson, and D. Bowtell. 1993. The SH2 and SH3 domains of mammalian Grb2 couple the EGF receptor to the Ras activator mSos1. Nature. 363:83-85. http://dx.doi.org/10.1038/363083a0
    • (1993) Nature. , vol.363 , pp. 83-85
    • Rozakis-Adcock, M.1    Fernley, R.2    Wade, J.3    Pawson, T.4    Bowtell, D.5
  • 39
    • 77958114168 scopus 로고    scopus 로고
    • FRS2α regulates Erk levels to control a self-renewal target Hes1 and proliferation of FGF-responsive neural stem/progenitor cells
    • Sato, T., T. Shimazaki, H. Naka, S. Fukami, Y. Satoh, H. Okano, I. Lax, J. Schlessinger, and N. Gotoh. 2010. FRS2α regulates Erk levels to control a self-renewal target Hes1 and proliferation of FGF-responsive neural stem/progenitor cells. Stem Cells. 28:1661-1673. http://dx.doi.org/10.1002/stem.488
    • (2010) Stem Cells. , vol.28 , pp. 1661-1673
    • Sato, T.1    Shimazaki, T.2    Naka, H.3    Fukami, S.4    Satoh, Y.5    Okano, H.6    Lax, I.7    Schlessinger, J.8    Gotoh, N.9
  • 40
    • 39749113704 scopus 로고    scopus 로고
    • Extracellular point mutations in FGFR2 result in elevated ERK1/2 activation and perturbation of neuronal differentiation
    • Schüller, A.C., Z. Ahmed, and J.E. Ladbury. 2008. Extracellular point mutations in FGFR2 result in elevated ERK1/2 activation and perturbation of neuronal differentiation. Biochem. J. 410:205-211. http://dx.doi.org/10.1042/BJ20070859
    • (2008) Biochem. J. , vol.410 , pp. 205-211
    • Schüller, A.C.1    Ahmed, Z.2    Ladbury, J.E.3
  • 41
    • 75149170979 scopus 로고    scopus 로고
    • Fibroblast growth factor signalling: from development to cancer
    • Turner, N., and R. Grose. 2010. Fibroblast growth factor signalling: from development to cancer. Nat. Rev. Cancer. 19:116-129. http://dx.doi.org/10.1038/nrc2780
    • (2010) Nat. Rev. Cancer. , vol.10 , pp. 116-129
    • Turner, N.1    Grose, R.2
  • 43
    • 34247871298 scopus 로고    scopus 로고
    • Distinct roles of fibroblast growth factor receptor 1 and 2 in regulating cell survival and epithelialmesenchymal transition
    • Xian, W., K.L. Schwertfeger, and J.M. Rosen. 2007. Distinct roles of fibroblast growth factor receptor 1 and 2 in regulating cell survival and epithelialmesenchymal transition. Mol. Endocrinol. 21:987-1000. http://dx.doi.org/10.1210/me.2006-0518
    • (2007) Mol. Endocrinol. , vol.21 , pp. 987-1000
    • Xian, W.1    Schwertfeger, K.L.2    Rosen, J.M.3
  • 44
    • 0034687699 scopus 로고    scopus 로고
    • Loss of fibroblast growth factor receptor 2 ligand-binding specificity in Apert syndrome
    • Yu, K., A.B. Herr, G. Waksman, and D.M. Ornitz. 2000. Loss of fibroblast growth factor receptor 2 ligand-binding specificity in Apert syndrome. Proc. Natl. Acad. Sci. USA. 97:14536-14541. http://dx.doi.org/10.1073/pnas.97.26.14536
    • (2000) Proc. Natl. Acad. Sci. USA. , vol.97 , pp. 14536-14541
    • Yu, K.1    Herr, A.B.2    Waksman, G.3    Ornitz, D.M.4

* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.