Expression of Gab1 Lacking the Pleckstrin Homology Domain Is Associated with Neoplastic Progression

REFERENCES

• Aaronson, S. A.. 1991. Growth factors and cancer. Science 254:1146–1153.
   PubMed Web of Science ®Google Scholar
• Afshari, C. A., and J. C. Barrett. 1993. Negative regulation of mitogen-stimulated, anchorage-independent cell growth by a tumor-suppressor gene function. Mol. Carcinog. 7:249–256.
   PubMedGoogle Scholar
• 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.
   PubMed Web of Science ®Google Scholar
• Barrett, J. C.. 1993. Mechanisms of multistep carcinogenesis and carcinogen risk assessment. Environ. Health Perspect. 100:9–20.
   PubMed Web of Science ®Google Scholar
• Barrett, J. C.. 1980. A preneoplastic stage in the spontaneous neoplastic transformation of Syrian hamster embryo cells in culture. Cancer Res. 40:91–94.
   PubMed Web of Science ®Google Scholar
• Barrett, J. C., B. D. Crawford, L. O. Mixter, L. M. Schechtman, P. O. P. Ts'o, and R. Pollack. 1979. Correlation of in vitro growth properties and tumorigenicity of Syrian hamster cell lines. Cancer Res. 39:1504–1510.
   PubMedGoogle Scholar
• Barrett, J. C., and P. O. P. Ts'o. 1978. Evidence for the progressive nature of neoplastic transformation in vitro. Proc. Natl. Acad. Sci. USA 75:3761–3765.
   PubMed Web of Science ®Google Scholar
• Barrett, J. C., A. Wong, and J. A. McLachlan. 1981. Diethylstilbestrol induces neoplastic transformation without measurable gene mutation at two loci. Science 212:1402–1404.
   PubMed Web of Science ®Google Scholar
• Boyd, J. A., and J. C. Barrett. 1990. Genetic and cellular basis of multistep carcinogenesis. Pharmacol. Ther. 46:469–486.
   PubMed Web of Science ®Google Scholar
• 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.
   PubMed Web of Science ®Google Scholar
• Deb, T. B., L. Wong, D. S. Salomon, G. Zhou, J. E. Dixon, J. S. Gutkind, S. A. Thompson, and G. R. Johnson. 1998. A common requirement for the catalytic activity and both SH2 domains of SHP-2 in mitogen-activated protein (MAP) kinase activation by the ErbB family of receptors. A specific role for SHP-2 in MAP, but not c-Jun amino-terminal kinase activation. J. Biol. Chem. 273:16643–16646.
   PubMed Web of Science ®Google Scholar
• 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, Cbl and Gab1. J. Biol. Chem. 272:20167–20172.
   PubMedGoogle Scholar
• Glasgow, W. C., C. A. Afshari, J. C. Barrett, and T. E. Eling. 1992. Modulation of the epidermal growth factor mitogenic response by metabolites of linoleic and arachidonic acid in Syrian hamster embryo fibroblasts. Differential effects in tumor suppressor gene (+) and (−) phenotypes. J. Biol. Chem. 267:10771–10779.
   PubMed Web of Science ®Google Scholar
• Glasgow, W. C., R. Hui, A. L. Everhart, S. P. Jayawickreme, J. Angerman-Stewart, B.-B. Han, and T. E. Eling. 1997. The linoleic acid metabolite, (13S)-hydroperoxyoctadecadienooic acid, augments the epidermal growth factor receptor signaling pathway by attenuation of receptor dephosphorylation. Differential response in Syrian hamster embryo tumor suppressor phenotypes. J. Biol. Chem. 272:19269–19276.
   PubMedGoogle Scholar
• Gu, H., J. C. Pratt, S. J. Burakoff, and B. G. Neel. 1998. Cloning of p97/Gab2, the major SHP2-binding protein in hematopoietic cells, reveals a novel pathway for cytokine-induced gene activation. Mol. Cell 2:729–740.
   PubMed Web of Science ®Google Scholar
• Hayflick, L.. 1976. The cell biology of human aging. N. Engl. J. Med. 295:1302–1308.
   PubMed Web of Science ®Google Scholar
• Herbst, R., P. M. Carroll, 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.
   PubMed Web of Science ®Google Scholar
• 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 signalling. Nature (London) 379:560–564.
   PubMed Web of Science ®Google Scholar
• Hui, R., H. Kameda, J. I. Risinger, J. Angerman-Stewart, B. Han, J. C. Barrett, T. E. Eling, and W. C. Glasgow. 1999. The linoleic acid metabolite, 13-HpODE augments the phosphorylation of EGF receptor and SHP-2 leading to their increased association. Prostaglandins Leukot. Essent. Fatty Acids 61:137–143.
   PubMedGoogle Scholar
• Isakoff, S. J., T. Cardozo, J. Andreev, Z. Li, K. M. Ferguson, R. Abagyan, M. A. Lemmon, A. Aronheim, and E. Y. Skolnik. 1998. Identification and analysis of PH domain-containing targets of phosphatidylinositol 3-kinase using a novel in vivo assay in yeast. EMBO J. 17:5374–5387.
   PubMed Web of Science ®Google Scholar
• Isfort, R. J., and R. A. LeBoeuf. 1995. The Syrian hamster embryo (SHE) cell transformation system: a biologically relevant in vitro model—with carcinogen predicting capabilities—of in vivo multistage neoplastic transformation. Crit. Rev. Oncogene 6:251–260.
   PubMedGoogle Scholar
• Itoh, M., Y. Yoshida, K. Nishida, M. Narimatsu, M. Hibi, and T. Hirano. 2000. Role of Gab1 in heart, placenta, and skin development and growth factor- and cytokine-induced extracellular signal-regulated kinase mitogen-activated protein kinase activation. Mol. Cell. Biol. 20:3695–3704.
   PubMed Web of Science ®Google Scholar
• Jones, N., and D. J. Dumont. 1998. The Tek/Tie2 receptor signals through a novel Dok-related docking protein, Dok-R. Oncogene 17:1097–1108.
   PubMedGoogle Scholar
• Kameda, H., J. I. Risinger, B.-B. Han, S. J. Baek, J. C. Barrett, W. C. Glasgow, and T. E. Eling. 2001. Identification of epidermal growth factor receptor-Grb2-associated binder-1-SHP-2 complex formation and its functional loss during neoplastic cell progression. Cell Growth Diff. 12:307–318.
   PubMedGoogle Scholar
• Kameda, H., I. Morita, M. Handa, J. Kaburaki, T. Yoshida, T. Mimori, S.-I. Murota, and Y. Ikeda. 1997. Reexpression of functional P-selectin molecules on the endothelial cell surface by repeated stimulation with thrombin. Br. J. Haematol. 97:348–355.
   PubMed Web of Science ®Google Scholar
• Koi, M., C. A. Afshari, L. A. Annab, and J. C. Barrett. 1989. Role of a tumor-suppressor gene in the negative control of anchorage-independent growth of Syrian hamster cells. Proc. Natl. Acad. Sci. USA 86:8773–8777.
   PubMedGoogle Scholar
• Koi, M., and J. C. Barrett. 1986. Loss of tumor-suppressive function during chemically induced neoplastic progression of Syrian hamster embryo cells. Proc. Natl. Acad. Sci. USA 83:5992–5996.
   PubMed Web of Science ®Google Scholar
• 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.
   PubMed Web of Science ®Google Scholar
• Laffargue, M., P. Raynal, A. Yart, C. Peres, R. Wetzker, S. Roche, B. Payrastre, and H. Chap. 1999. An epidermal growth factor receptor/Gab1 signaling pathway is required for activation of phosphoinositide 3-kinase by lysophosphatidic acid. J. Biol. Chem. 274:32835–32841.
   PubMedGoogle Scholar
• Lehr, S., J. Kotzka, A. Herkner, E. Klein, C. Siethoff, B. Knebel, V. Noelle, J. C. Brüning, H. W. Klein, H. E. Meyer, W. Krone, and D. Müller-Wieland. 1999. Identification of tyrosine phosphorylation sites in human Gab-1 protein by EGF receptor kinase in vitro. Biochemistry 38:151–159.
   PubMed Web of Science ®Google Scholar
• 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.
   PubMed Web of Science ®Google Scholar
• Maroun, C. R., M. Holgado-Madruga, I. Royal, M. A. Naujokas, T. M. Fournier, A. J. Wong, and M. Park. 1999. 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. Mol. Cell. Biol. 19:1784–1799.
   PubMed Web of Science ®Google Scholar
• Maroun, C. R., D. K. Moscatello, M. A. Naujokas, M. Holgado-Madruga, A. J. Wong, and M. Park. 1999. A conserved inositol phospholipid binding site within the pleckstrin homology domain of the Gab1 docking protein is required for epithelial morphogenesis. J. Biol. Chem. 274:31719–31726.
   PubMedGoogle Scholar
• Newbold, R. F., R. W. Overell, and J. R. Connell. 1982. Induction of immortality is an early event in malignant transformation of mammalian cells by carcinogens. Nature (London) 299:633–635.
   PubMed Web of Science ®Google Scholar
• Nishida, K., Y. Yoshida, M. Itoh, T. Fukada, T. Ohtani, T. Shirogane, T. Atsumi, M. Takahashi-Tezuka, K. Ishihara, M. Hibi, and T. Hirano. 1999. Gab-family adapter proteins act downstream of cytokine and growth factor receptors and T- and B-cell antigen receptors. Blood 93:1809–1816.
   PubMed Web of Science ®Google Scholar
• Oshimura, M., T. W. Hesterberg, T. Tsutsui, and J. C. Barrett. 1984. Correlation of asbestos-induced cytogenetic effects with cell transformation of Syrian hamster embryo cells in culture. Cancer Res. 44:5017–5022.
   PubMed Web of Science ®Google Scholar
• Qu, C.-K., W.-M. Yu, B. Azzarelli, and G.-S. Feng. 1999. Genetic evidence that Shp-2 tyrosine phosphatase is a signal enhancer of the epidermal growth factor receptor in mammals. Proc. Natl. Acad. Sci. USA 96:8528–8533.
   PubMedGoogle Scholar
• Raabe, T., J. Riesgo-Escovar, X. Liu, B. S. Bausenwein, P. Deak, P. Maröy, 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.
   PubMed Web of Science ®Google Scholar
• Rebecchi, M. J., and S. Scarlata. 1998. Pleckstrin homology domains: a common fold with diverse functions. Annu. Rev. Biophys. Biomol. Struct. 27:503–528.
   PubMedGoogle Scholar
• Rodrigues, G. A., M. Falasca, Z. Zhang, S. H. Ong, and J. Schlessinger. 2000. A novel positive feedback loop mediated by the docking protein Gab1 and phosphatidylinositol 3-kinase in epidermal growth factor receptor signaling. Mol. Cell. Biol. 20:1448–1459.
   PubMedGoogle Scholar
• Shi, Z.-Q., D.-H. Yu, M. Park, M. Marshall, and G.-S. Feng. 2000. Molecular mechanism for the Shp-2 tyrosine phosphatase function in promoting growth factor stimulation of Erk activity. Mol. Cell. Biol. 20:1526–1536.
   PubMedGoogle Scholar
• Takahashi-Tezuka, M., Y. Yoshida, T. Fukada, T. Ohtani, Y. Yamanaka, K. Nishida, K. Nakajima, M. Hibi, and T. Hirano. 1998. Gab1 acts as an adapter molecule linking the cytokine receptor gp130 to ERK mitogen-activated protein kinase. Mol. Cell. Biol. 18:4109–4117.
   PubMed Web of Science ®Google Scholar
• Weidner, K. M., S. Di Cesare, M. Sachs, V. Brinkmann, J. Behrens, and W. Birchmeier. 1996. Interaction between Gab1 and the c-Met receptor tyrosine kinase is responsible for epithelial morphogenesis. Nature (London) 384:173–176.
   PubMed Web of Science ®Google Scholar
• Yamanashi, Y., and D. Baltimore. 1997. Identification of the Abl- and rasGAP-associated 62 kDa protein as a docking protein, Dok. Cell 88:205–211.
   PubMed Web of Science ®Google Scholar
• Yenush, L., and M. F. White. 1997. The IRS-signalling system during insulin and cytokine action. Bioessays 19:491–500.
   PubMed Web of Science ®Google Scholar
• Zhao, C., D.-H. Yu, R. Shen, and G.-S. Feng. 1999. Gab2, a new pleckstrin homology domain-containing adapter protein, acts to uncouple signaling from ERK kinase to Elk-1. J. Biol. Chem. 274:19649–19654.
   PubMed Web of Science ®Google Scholar