Functional interaction between RhoB and the transcription factor DB1

References

• Adamson P., Marshall C. J., Hall A., Tilbrook P. A. Post-translational modification of p21rho proteins. J. Biol. Chem. 1992a; 267: 20033–20038
   PubMed Web of Science ®Google Scholar
• Adamson P., Paterson H. F., Hall A. Intracellular localization of the p21rho proteins. J. Cell Biol. 1992b; 119: 617–627
   PubMed Web of Science ®Google Scholar
• Burridge K., Chrzanowska-Wodnicka M. Focal adhesions, contractility, and signaling. Ann. Rev. Cell Dev. Biol. 1996; 12: 463–518
   PubMed Web of Science ®Google Scholar
• Casey P. J., Seabra M. C. Protein prenyltransferases. J. Biol. Chem. 1996; 271: 5289–5292
   PubMed Web of Science ®Google Scholar
• Chen C., Okayama H. High efficiency transformation of mammalian cells by plasmid DNA. Mol. Cell Biol. 1987; 7: 2745–2752
   PubMed Web of Science ®Google Scholar
• Cox A. D., Der C. J. Protein prenylation: more than just glue. Curr. Opin. Cell Biol. 1992; 4: 1008–1016
   PubMedGoogle Scholar
• Fukumoto Y., Kaibuchi K., Hori Y., Fujioka H., Araki S., Ueda T., Kikuchi A., Takai Y. Molecular cloning and characterization of a novel type of regulatory protein (GDI) for the rho proteins, ras p21-like GTP-binding proteins. Oncogene. 1990; 5: 1321–1328
   PubMed Web of Science ®Google Scholar
• Gibbs J., Oliff A., Kohl N. E. Farnesyltransferase inhibitors: Ras research yields a potential cancer therapeutic. Cell 1994; 77: 175–178
   PubMed Web of Science ®Google Scholar
• Hall A. Small GTP-binding proteins and the regulation of the actin cytoskeleton. Ann. Rev. Cell Biol. 1994; 10: 31–54
   PubMedGoogle Scholar
• Harlow E., Lane D. Antibodies: A Laboratory Manual. Cold Spring Harbor Press, Cold Spring Harbor, NY 1988
   Google Scholar
• Hill C. S., Wynne J., Treisman R. The Rho family GTPases RhoA, Racl, and CDC42Hs regulate transcriptional activation by SRF. Cell 1995; 81: 1159–1170
   PubMed Web of Science ®Google Scholar
• Hori Y., Kikuchi A., Isomura M., Katayama M., Miura Y., Fujioka H., Kaibuchi K., Takai Y. Posttranslational modifications of the C-terminal region of the rho protein are important for its interaction with membranes and the stimulatory and inhibitory GDP/GTP exchange proteins. Oncogene. 1991; 6: 515–522
   PubMed Web of Science ®Google Scholar
• Hotchin N. A., Hall A. Regulation of the actin cytoskeleton, integrins and cell growth by the Rho family of small GTPases. Cancer Surv. 1996; 27: 311–322
   PubMedGoogle Scholar
• Isomura M., Kikuchi A., Ohga N., Takai Y. Regulation of binding of rhoB p20 to membranes by its specific regulatory protein, GDP dissociation inhibitor. Oncogene. 1991; 6: 119–124
   PubMed Web of Science ®Google Scholar
• Jahner D., Hunter T. The ras. related gene rho B. is an immediate-early gene inducible by v-Fps, epidermal growth factor, and platelet-derived growth factor in rat fibroblasts. Mol. Cell Biol. 1991a; 11: 3682–3690
   PubMed Web of Science ®Google Scholar
• Jahner D., Hunter T. The stimulation of quiescent rat fibroblasts by v-src and v-fps. oncogenic protein-tyrosine kinases leads to the induction of a subset of immediate early genes. Oncogene. 1991b; 6: 1259–1268
   PubMed Web of Science ®Google Scholar
• Kohl N. E., Redner F., Mosser S., Guiliani E. A., deSolms S. J., Conner M. W., Anthony N. J., Holtz W. J., Gomez R. P.T., Lee J., Smith R. L., Graham S. L., Hartman G. D., Gibbs J., Oliff A. Protein farnesyltransferase inhibitors block the growth of ras-dependent tumors in nude mice. Proc. Natl. Acad. Sci. USA 1994; 91: 9141–9145
   PubMed Web of Science ®Google Scholar
• Koyano-Nakagawa N., Nishida J., Baldwin D., Arai K.-L., Yokota T. Molecular cloning of a novel human cDNA encoding a zinc finger protein that binds to the interleukin-3 promoter. Mol. Cell Biol. 1994; 14: 5099–5107
   PubMed Web of Science ®Google Scholar
• Lamaze C., Chuang T.-H., Terlecky L. J., Bokoch G. M., Schmid S. L. Regulation of receptor-mediated endocytosis by Rho and Rac. Nature 1996; 382: 177–179
   PubMed Web of Science ®Google Scholar
• Larochelle D. A., Vithalani K. K., DeLozanne A. A novel member of the rho family of small GTP-binding proteins is specifically required cytokinesis. J. Cell Biol. 1996; 133: 1321–1329
   PubMed Web of Science ®Google Scholar
• Lebowitz P., Casey P. J., Prendergast G. C., Thissen J. Farnesyltransferase inhibitors alter the prenylation and growth-stimulating function of Rho B. J. Biol. Chem. 1997a; 272: 15591–15594
   PubMed Web of Science ®Google Scholar
• Lebowitz P., Du W., Prendergast G. C. Prenylation of RhoB is required for its cell transforming functions but not its ability to activate SRE-dependent transcription. J. Biol. Chem. 1997b; 272: 16093–16096
   PubMed Web of Science ®Google Scholar
• Lebowitz P. F., Sakamuro D., Prendergast G. C. Farnesyltransferase inhibitors induce apoptosis in Ras-transformed cells denied substratum attachment. Cancer Res. 1997c; 57: 708–713
   PubMed Web of Science ®Google Scholar
• Lebowitz P. F., Davide J. P., Prendergast G. C. Evidence that farnesyl transferase inhibitors suppress Ras transformation by interfering with Rho activity. Mol. Cell Biol. 1995; 15: 6613–6622
   PubMed Web of Science ®Google Scholar
• Lin H.-J., Eviner V., Prendergast G. C., White E. Activated H-ras., rescues EIA-induced apoptosis and co-operates with E1A to overcome p53-dependent growth arrest. Mol. Cell Biol. 1995; 15: 4536–4544
   PubMed Web of Science ®Google Scholar
• Margolin J. F., Friedman J. R., Meyer W. K., Vissing H., Thiesen H. J.F.J., Rauscher I II. Kruppel-associated boxes are potent transcriptional repression domains. Proc. Natl. Acad. Sci. USA 1994; 91: 4509–4513
   PubMed Web of Science ®Google Scholar
• Marshall C. J. Protein prenylation: a mediator of protein-protein interactions. Science 1993; 259: 1865–1866
   PubMed Web of Science ®Google Scholar
• Murphy D., Saffrich R., Grummt M., Gournier H., Rybin V., Rubino M., Auvinen P., Lütcke A., Parton R. G., Zerial M. Endosome dynamics regulated by a Rho protein. Nature 1996; 384: 427–432
   PubMed Web of Science ®Google Scholar
• Murre C., Mc P. S., BaltimoreCaw D. A new DNA-binding and dimerization motif in immunoglobulin enhancer binding, daughterless, MyoD, and Myc proteins. Cell 1989; 56: 777–783
   PubMed Web of Science ®Google Scholar
• Paterson H. F., Self A. J., Garrett M. D., Just I., Aktories K., Hall A. Microinjection of recombinant p21rho induces rapid changes in cell morphology. J. Cell Biol. 1990; 111: 1001–1007
   PubMed Web of Science ®Google Scholar
• Prendergast G. C., Khosravi-Far R., Solski P., Kurzawa H., Lebowitz P., Der C. J. Critical role of Rho in cell transformation by oncogenic Ras. Oncogene. 1995; 10: 2289–2296
   PubMed Web of Science ®Google Scholar
• Prendergast G. C., Ziff E. B. Mbhl: A novel gelsolin/ severin-related protein which binds actin in vitro., and exhibits nuclear localization in vivo. EMBO J. 1991; 10: 757–766
   PubMed Web of Science ®Google Scholar
• Ridley A. J. Rho-related proteins: actin cytoskeleton and cell cycle. Curr. Opin. Genet. Dev. 1995; 5: 24–30
   PubMed Web of Science ®Google Scholar
• Ridley A. J. Rho: theme and variations. Curr. Biol. 1996; 6: 1256–1264
   PubMed Web of Science ®Google Scholar
• Schmalzing G., Richter H. P., Hansen A., Schwarz W., Just I., Aktories K. Involvement of the GTP binding protein Rho in constitutive endocytosis in Xenopus laevis oocytes. J. Cell Biol. 1995; 130: 1319–1332
   PubMed Web of Science ®Google Scholar
• Schwartz M. A., Schaller M. D., Ginsberg M. H. Integrins: emerging paradigms of signal transduction. Ann. Rev. Cell Dev. Biol. 1995; 11: 549–599
   PubMed Web of Science ®Google Scholar
• Self A. J., Paterson H. F., Hall A. Different structural organization of Ras and Rho effector domains. Oncogene. 1993; 8: 655–661
   PubMed Web of Science ®Google Scholar
• Shih T. Y., Stokes P. E., Smythers G. W., Dhar R., Oroszlan S. Characterization of the phosphorylation sites and the surrounding amino acid sequences of the p21 transforming proteins coded for by the Harvey and Kirsten strains of murine sarcoma viruses. J. Biol. Chem. 1982; 257: 11767–11773
   PubMed Web of Science ®Google Scholar
• Symons M. Rho family GTPases: the cytoskeleton and beyond. Trends Biochem. Sci. 1996; 21: 178–181
   PubMed Web of Science ®Google Scholar
• Tapon N., Hall A. Rho, Rac and Cdc42 GTPases regulate the organization of the actin cytoskeleton. Curr. Opin. Cell Biol. 1997; 9: 86–92
   PubMed Web of Science ®Google Scholar
• Ueda T., Kikuchi A., Ohga N., Yamamoto J., Takai Y. Purification and characterization from bovine brain cytosol of a novel regulatory protein inhibiting the dissociation of GDP from and the subsequence binding of GTP to rhoB p20, a ras p21-like GTP binding protein. J. Biol. Chem. 1990; 265: 9373–9380
   PubMed Web of Science ®Google Scholar
• Vojtek A. B., Hollenberg S. M., Cooper J. A. Mammalian ras interacts directly with the serine/threonine kinase Raf. Cell 1993; 74: 205–214
   PubMed Web of Science ®Google Scholar
• Wu W. J., Leonard D. A., Cerione R., Manor D. Interaction between Cdc42Hs and RhoGDI is mediated through the Rho insert region. J. Biol. Chem. 1997; 272: 26153–26158
   PubMed Web of Science ®Google Scholar
• Zalcman G., Closson V., Camonis J., Honore N., Rousseau-Merck M. F., Tavitian A., Olofsson B. RhoGDI-3 is a new GDP dissociation inhibitor (GDI). Identification of a non-cytosolic GDI protein interacting with the small GTP-binding proteins RhoB and RhoG. J. Biol. Chem. 1996; 271: 30366–30374
   PubMed Web of Science ®Google Scholar
• Zalcman G., Closson V., Linares-Cruz G., Leregours F., Honore N., Tavitian A., Olofsson B. Regulation of Ras-related RhoB protein expression during the cell cycle. Oncogene. 1995; 10: 1935–1945
   PubMed Web of Science ®Google Scholar
• Zhang F. L., Casey P. J. Protein prenylation: molecular mechanisms and functional consequences. Ann. Rev. Biochem. 1996; 65: 241–269
   PubMed Web of Science ®Google Scholar
• Zigmond S. H. Signal transduction and actin filament organization. Curr. Opin. Cell Biol. 1996; 8: 66–73
   PubMed Web of Science ®Google Scholar