Inhibition of the Motility and Growth of B16F10 Mouse Melanoma Cells by Dominant Negative Mutants of Dok-1

REFERENCES

• Bouton, A. H., S. B. Kanner, R. R. Vines, H. C. Wang, J. B. Gibbs, and J. T. Parsons. 1991. Transformation by pp60src or stimulation of cells with epidermal growth factor induces the stable association of tyrosine-phosphorylated cellular proteins with GTPase-activating protein. Mol. Cell. Biol. 11:945–953.
   PubMedGoogle Scholar
• Carpino, N., D. Wisniewski, A. Strife, D. Marshak, R. Kobayashi, B. Stillman, and B. Clarkson. 1997. p62(dok): a constitutively tyrosine-phosphorylated, GAP-associated protein in chronic myelogenous leukemia progenitor cells. Cell 88:197–204.
   PubMed Web of Science ®Google Scholar
• Clark, E. A., W. G. King, J. S. Brugge, M. Symons, and R. O. Hynes. 1998. Integrin-mediated signals regulated by members of the Rho family of GTPases. J. Cell Biol. 142:573–586.
   PubMed Web of Science ®Google Scholar
• Cong, F., B. Yuan, and S. P. Goff. 1999. Characterization of a novel member of the DOK family that binds and modulates Abl signaling. Mol. Cell. Biol. 19:8314–8325.
   PubMedGoogle Scholar
• DeClue, J. E., W. C. Vass, M. R. Johnson, D. W. Stacey, and D. R. Lowy. 1993. Functional role of GTPase-activating protein in cell transformation by pp60v-src. Mol. Cell. Biol. 13:6799–6809.
   PubMedGoogle Scholar
• Di Cristofano, A., N. Carpino, N. Dunant, G. Friedland, R. Kobayashi, A. Strife, D. Wisniewski, B. Clarkson, P. P. Pandolfi, and M. D. Resh. 1998. Molecular cloning and characterization of p56dok-2 defines a new family of RasGAP-binding proteins. J. Biol. Chem. 273:4827–4830.
   PubMedGoogle Scholar
• Ellis, C., M. Moran, F. McCormick, and T. Pawson. 1990. Phosphorylation of GAP and GAP-associated proteins by transforming and mitogenic tyrosine kinases. Nature 343:377–381.
   PubMed Web of Science ®Google Scholar
• Fidler, I.. 1973. Selection of successive tumour lines for metastasis. Nat. New Biol. 242:148–149.
   PubMedGoogle Scholar
• Fincham, V. J., M. Unlu, V. G. Brunton, J. D. Pitts, J. A. Wyke, and M. C. Frame. 1996. Translocation of Src kinase to the cell periphery is mediated by the actin cytoskeleton under the control of the Rho family of small G proteins. J. Cell Biol. 135:1551–1564.
   PubMedGoogle Scholar
• Fincham, V. J., A. Chudleigh, and M. C. Frame. 1999. Regulation of p190 Rho-GAP by v-Src is linked to cytoskeletal disruption during transformation. J. Cell Sci. 112:947–956.
   PubMedGoogle Scholar
• Fox, P. L., G. Sa, S. F. Dobrowolski, and D. W. Stacey. 1994. The regulation of endothelial cell motility by p21 ras. Oncogene 9:3519–3526.
   PubMedGoogle Scholar
• Fujita, M., D. A. Norris, H. Yagi, P. Walsh, J. G. Morelli, W. L. Weston, N. Terada, S. D. Bennion, W. Robinson, M. Lemon, I. H. Maxwell, and J. J. Yohn. 1999. Overexpression of mutant ras in human melanoma increases invasiveness, proliferation and anchorage-independent growth in vitro and induces tumour formation and cachexia in vivo. Melanoma Res. 9:279–291.
   PubMedGoogle Scholar
• Hanahan, D., and R. A. Weinberg. 2000. The hallmarks of cancer. Cell 100:57–70.
   PubMed Web of Science ®Google Scholar
• Hill, R. P., A. F. Chambers, V. Ling, and J. F. Harris. 1984. Dynamic heterogeneity: rapid generation of metastatic variants in mouse B16 melanoma cells. Science 224:998–1001.
   PubMedGoogle Scholar
• Hu, K. Q., and J. Settleman. 1997. Tandem SH2 binding sites mediate the RasGAP-RhoGAP interaction: a conformational mechanism for SH3 domain regulation. EMBO J. 16:473–483.
   PubMedGoogle 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
• Jones, N., and D. J. Dumont. 1999. Recruitment of Dok-R to the EGF receptor through its PTB domain is required for attenuation of Erk MAP kinase activation. Curr. Biol. 9:1057–1060.
   PubMedGoogle Scholar
• Kashige, N., N. Carpino, and R. Kobayashi. 2000. Tyrosine phosphorylation of p62dok by p210bcr-abl inhibits RasGAP activity. Proc. Natl. Acad. Sci. USA 97:2093–2098.
   PubMedGoogle Scholar
• Klemke, R. L., S. Cai, A. L. Giannini, P. J. Gallagher, P. de Lanerolle, and D. A. Cheresh. 1997. Regulation of cell motility by mitogen-activated protein kinase. J. Cell Biol. 137:481–492.
   PubMed Web of Science ®Google Scholar
• Lauffenburger, D. A., and A. F. Horwitz. 1996. Cell migration: a physically integrated molecular process. Cell 84:359–369.
   PubMed Web of Science ®Google Scholar
• Leblanc, V., B. Tocque, and I. Delumeau. 1998. Ras-GAP controls Rho-mediated cytoskeletal reorganization through its SH3 domain. Mol. Cell. Biol. 18:5567–5578.
   PubMed Web of Science ®Google Scholar
• Lemay, S., D. Davidson, S. Latour, and A. Veillette. 2000. Dok-3, a novel adapter molecule involved in the negative regulation of immunoreceptor signaling. Mol. Cell. Biol. 20:2743–2754.
   PubMed Web of Science ®Google Scholar
• Lock, P., F. Casagranda, and A. R. Dunn. 1999. Independent SH2-binding sites mediate interaction of Dok-related protein with RasGTPase-activating protein and Nck. J. Biol. Chem. 274:22775–22784.
   PubMed Web of Science ®Google Scholar
• Lu, W., S. Katz, R. Gupta, and B. J. Mayer. 1997. Activation of Pak by membrane localization mediated by an SH3 domain from the adaptor protein Nck. Curr. Biol. 7:85–94.
   PubMed Web of Science ®Google Scholar
• Lugo, T. G., A. M. Pendergast, A. J. Muller, and O. N. Witte. 1990. Tyrosine kinase activity and transformation potency of bcr-abl oncogene products. Science 247:1079–1082.
   PubMed Web of Science ®Google Scholar
• Mitchison, T. J., and L. P. Cramer. 1996. Actin-based cell motility and cell locomotion. Cell 84:371–379.
   PubMed Web of Science ®Google Scholar
• Moran, M. F., P. Polakis, F. McCormick, T. Pawson, and C. Ellis. 1991. Protein-tyrosine kinases regulate the phosphorylation, protein interactions, subcellular distribution, and activity of p21ras GTPase-activating protein. Mol. Cell. Biol. 11:1804–1812.
   PubMed Web of Science ®Google Scholar
• Mulcahy, L. S., M. R. Smith, and D. W. Stacey. 1985. Requirement for ras proto-oncogene function during serum-stimulated growth of NIH 3T3 cells. Nature 313:241–243.
   PubMed Web of Science ®Google Scholar
• Nelms, K., A. L. Snow, J. Hu-Li, and W. E. Paul. 1998. FRIP, a hematopoietic cell-specific rasGAP-interacting protein phosphorylated in response to cytokine stimulation. Immunity 9:13–24.
   PubMedGoogle Scholar
• Nobes, C. D., and A. Hall. 1999. Rho GTPases control polarity, protrusion, and adhesion during cell movement. J. Cell Biol. 144:1235–1244.
   PubMed Web of Science ®Google Scholar
• Noguchi, T., T. Matozaki, K. Inagaki, M. Tsuda, K. Fukunaga, Y. Kitamura, T. Kitamura, K. Shii, Y. Yamanashi, and M. Kasuga. 1999. Tyrosine phosphorylation of p62(Dok) induced by cell adhesion and insulin: possible role in cell migration. EMBO J. 18:1748–1760.
   PubMed Web of Science ®Google Scholar
• Rafnar, T., R. S. Peebles, M. E. Brummet, B. Catipovic, F. Imani, D. W. MacGlashan, and D. G. Marsh. 1998. Stimulation of the high-affinity IgE receptor results in the tyrosine phosphorylation of a 60 kD protein which is associated with the protein-tyrosine kinase, Csk. Mol. Immunol. 35:249–257.
   PubMedGoogle Scholar
• Ridley, A. J., P. M. Comoglio, and A. Hall. 1995. Regulation of scatter factor/hepatocyte growth factor responses by Ras, Rac, and Rho in MDCK cells. Mol. Cell. Biol. 15:1110–1122.
   PubMed Web of Science ®Google Scholar
• Ridley, A. J., W. E. Allen, M. Peppelenbosch, and G. E. Jones. 1999. Rho family proteins and cell migration. Biochem. Soc. Symp. 65:111–123.
   PubMedGoogle Scholar
• Schwarzbauer, J. E.. 1997. Cell migration: may the force be with you. Curr. Biol. 7:292–294.
   PubMed Web of Science ®Google Scholar
• Shellman, Y. G., J. T. Chapman, M. Fujita, D. A. Norris, and I. H. Maxwell. 2000. Expression of activated N-ras in a primary melanoma cell line counteracts growth inhibition by transforming growth factor-beta. J. Investig. Dermatol. 114:1200–1204.
   PubMedGoogle Scholar
• Songyang, Z., Y. Yamanashi, D. Liu, and D. Baltimore. 2001. Domain-dependent function of the rasGAP-binding protein p62Dok in cell signaling. J. Biol. Chem. 276:2459–2465.
   PubMedGoogle Scholar
• Suzu, S., M. Tanaka-Douzono, K. Nomaguchi, M. Yamada, H. Hayasawa, F. Kimura, and K. Motoyoshi. 2000. p56(dok-2) as a cytokine-inducible inhibitor of cell proliferation and signal transduction. EMBO J. 19:5114–5122.
   PubMed Web of Science ®Google Scholar
• Sylla, B. S., K. Murphy, E. Cahir-McFarland, W. S. Lane, G. Mosialos, and E. Kieff. 2000. The X-1inked lymphoproliferative syndrome gene product SH2D1A associates with p62dok (Dok1) and activates NF-κB. Proc. Natl. Acad. Sci. USA 97:7470–7475.
   PubMed Web of Science ®Google Scholar
• Tamir, I., J. C. Stolpa, C. D. Helgason, K. Nakamura, P. Bruhns, M. Daeron, and J. C. Cambier. 2000. The RasGAP-binding protein p62dok is a mediator of inhibitory FcγRIIB signals in B cells. Immunity 12:347–358.
   PubMed Web of Science ®Google Scholar
• Tang, J., G.-S. Feng, and W. Li. 1997. Induced direct binding of the adapter protein Nck to the GTPase-activating protein-associated protein p62 by epidermal growth factor. Oncogene 15:1823–1832.
   PubMedGoogle Scholar
• Vuica, M., S. Desiderio, and J. P. Schneck. 1997. Differential effects of B cell receptor and B cell receptor-FcγRIIB1 engagement on docking of Csk to GTPase-activating protein (GAP)-associated p62. J. Exp. Med. 186:259–267.
   PubMedGoogle Scholar
• White, M. F.. 1998. The IRS-signalling system: a network of docking proteins that mediate insulin action. Mol. Cell. Biochem. 182:3–11.
   PubMed Web of Science ®Google Scholar
• Wisniewski, D., A. Strife, D. Wojciechowicz, C. Lambek, and B. Clarkson. 1994. A 62-kilodalton tyrosine phosphoprotein constitutively present in primary chronic phase chronic myelogenous leukemia enriched lineage negative blast populations. Leukemia 8:688–693.
   PubMedGoogle 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
• Yamanashi, Y., T. Tamura, T. Kanamori, H. Yamane, H. Nariuchi, T. Yamamoto, and D. Baltimore. 2000. Role of the rasGAP-associated docking protein p62(dok) in negative regulation of B cell receptor-mediated signaling. Genes Dev. 14:11–16.
   PubMed Web of Science ®Google Scholar
• Yoshida, K., Y. Yamashita, A. Miyazato, K. Ohya, A. Kitanaka, U. Ikeda, K. Shimada, T. Yamanaka, K. Ozawa, and H. Mano. 2000. Mediation by the protein-tyrosine kinase Tec of signaling between the B cell antigen receptor and Dok-1. J. Biol. Chem. 275:24945–24952.
   PubMedGoogle Scholar
• Zaffran, Y., J. C. Escallier, S. Ruta, C. Capo, and J. L. Mege. 1995. Zymosan-triggered association of tyrosine phosphoproteins and lyn kinase with cytoskeleton in human monocytes. J. Immunol. 154:3488–3497.
   PubMedGoogle Scholar