Actin' up: RhoB in cancer and apoptosis (original) (raw)

• Van Aelst, L. & D'Souza-Schorey, C. Rho GTPases and signaling networks. Genes Dev. 11, 2295–2322 (1997).
  Article CAS Google Scholar
• Ridley, A. J. Rho proteins: linking signaling with membrane trafficking. Traffic 2, 303–310 (2001).
  Article CAS Google Scholar
• Wu, W. J., Erickson, J. W., Lin, R. & Cerione, R. A. The β-subunit of the coatomer complex binds Cdc42 to mediate transformation. Nature 405, 800–804 (2000).
  Article CAS Google Scholar
• Adamson, P., Paterson, H. F. & Hall, A. Intracellular localization of the p21rho proteins. J. Cell Biol. 119, 617–627 (1992).
  Article CAS Google Scholar
• Lebowitz, P. F., Davide, J. P. & Prendergast, G. C. Evidence that farnesyltransferase inhibitors suppress Ras transformation by interfering with Rho activity. Mol. Cell. Biol. 15, 6613–6622 (1995).
  Article CAS Google Scholar
• Zalcman, G. et al. Regulation of Ras-related RhoB protein expression during the cell cycle. Oncogene 10, 1935–1945 (1995).
  CAS PubMed Google Scholar
• Lebowitz, P. & Prendergast, G. C. Functional interaction between RhoB and the transcription factor DB1. Cell Adhes Commun 6, 277–287 (1998).
  Article CAS Google Scholar
• Michaelson, D. et al. Differential localization of Rho GTPases in live cells: regulation by hypervariable regions and RhoGDI binding. J. Cell Biol. 152, 111–126 (2001).
  Article CAS Google Scholar
• Mellor, J., Flynn, P., Nobes, C. D., Hall, A. & Parker, P. J. Prk1 is targeted to endosomes by the small GTPase, RhoB. J. Biol. Chem. 273, 4811–4814 (1998).
  Article CAS Google Scholar
• Gampel, A., Parker, P. J. & Mellor, H. Regulation of epidermal growth factor receptor traffic by the small GTPase RhoB. Curr. Biol. 9, 955–958 (1999).
  Article CAS Google Scholar
• Jahner, D. & Hunter, T. The _ras_-related gene RhoB is an immediate-early gene inducible by v-Fps, epidermal growth factor, and platelet-derived growth factor in rat fibroblasts. Mol. Cell. Biol. 11, 3682–3690 (1991).
  Article CAS Google Scholar
• Fritz, G., Kaina, B. & Aktories, K. The ras-related small GTP-binding protein RhoB is immediate-early inducible by DNA damaging treatments. J. Biol. Chem. 270, 25172–25177 (1995).
  Article CAS Google Scholar
• Engel, M. E., Datta, P. K. & Moses, H. L. RhoB is stabilized by transforming growth factor-β and antagonizes transcriptional activation. J. Biol. Chem. 273, 9921–9926 (1998).
  Article CAS Google Scholar
• Trapp, T. et al. GTPase RhoB: an early predictor of neuronal death after transient focal ischemia in mice. Mol. Cell. Neurosci. 17, 883–894 (2001).
  Article CAS Google Scholar
• Lebowitz, P., Casey, P. J., Prendergast, G. C. & Thissen, J. Farnesyltransferase inhibitors alter the prenylation and growth-stimulating function of RhoB. J. Biol. Chem. 272, 15591–15594 (1997).
  Article CAS Google Scholar
• Prendergast, G. C. et al. Critical role of Rho in cell transformation by oncogenic Ras. Oncogene 10, 2289–2296 (1995).
  CAS PubMed Google Scholar
• Du, W., Lebowitz, P. & Prendergast, G. C. Cell growth inhibition by farnesyltransferase inhibitors is mediated by gain of geranylgeranylated RhoB. Mol. Cell. Biol. 19, 1831–1840 (1999).
  Article CAS Google Scholar
• Du, W. & Prendergast, G. C. Geranylgeranylated RhoB mediates inhibition of human tumor cell growth by farnesyltransferase inhibitors. Cancer Res. 59, 5492–5496 (1999).
  CAS PubMed Google Scholar
• Chen, Z. et al. Both farnesylated and geranylgeranylated RhoB inhibit malignant transformation and suppress human tumor growth in nude mice. J. Biol. Chem. 275, 17974–17978 (2000).
  Article CAS Google Scholar
• Liu, A.-X., Rane, N., Liu, J.-P. & Prendergast, G. C. RhoB is dispensable for mouse development, but it modifies susceptibility to tumor formation as well as cell adhesion and growth factor signaling in transformed cells. Mol. Cell. Biol. 21, 6906–6912 (2001).
  Article CAS Google Scholar
• Khosravi-Far, R., Solski, P. A., Clark, G. J., Kinch, M. S. & Der, C. J. Activation of Rac1, RhoA, and mitogen-activated protein kinase are required for Ras transformation. Mol. Cell. Biol. 15, 6443–6453 (1995).
  Article CAS Google Scholar
• van Golen, K. L., Wu, Z.-F., Qiao, X. T., Bao, L. W. & Marajver, S. D. RhoC GTPase, a novel transforming oncogene for human mammary epithelial cells that partially recapitulates the inflammatory breast cancer phenotype. Cancer Res. 60, 5832–5838 (2000).
  CAS PubMed Google Scholar
• Lebowitz, P. F. & Prendergast, G. C. Non-Ras targets for farnesyltransferase inhibitors: focus on Rho. Oncogene 17, 1439–1447 (1998).
  Article CAS Google Scholar
• Prendergast, G. C. Farnesyltransferase inhibitors: antineoplastic mechanism and clinical prospects. Curr. Opin. Cell Biol. 12, 166–173 (2000).
  Article CAS Google Scholar
• Cox, A. D. & Der, C. J. Farnesyltransferase inhibitors and cancer treatment: targeting simply Ras? Biochim. Biophys. Acta 1333, F51–F71 (1997).
  CAS Google Scholar
• Prendergast, G. C. & Du, W. Targeting farnesyltransferase: is Ras relevant? Drug Resist. Updat 2, 81–84 (1999).
  Article CAS Google Scholar
• Rowinsky, E. K., Windle, J. J. & Von Hoff, D. D. Ras protein farnesyltransferase: a strategic target for anticancer therapeutic development. J. Clin. Oncol. 17, 3631–3652 (1999).
  Article CAS Google Scholar
• Sebti, S. M. & Hamilton, A. D. Farnesyltransferase and geranylgeranyltransferase I inhibitors and cancer therapy: lessons from mechanism and bench-to-bedside translational studies. Oncogene 19, 6584–6593 (2000).
  Article CAS Google Scholar
• Prendergast, G. C. & Oliff, A. Farnesyltransferase inhibitors: antineoplastic properties, mechanisms of action, and clinical prospects. Semin. Cancer Biol. 10, 443–452 (2000).
  Article CAS Google Scholar
• Adjei, A. A. Blocking oncogenic Ras signaling for cancer therapy. J. Natl Cancer Inst. 93, 1062–1074 (2001).
  Article CAS Google Scholar
• Prendergast, G. C. et al. Farnesyltransferase inhibition causes morphological reversion of _ras_-transformed cells by a complex mechanism that involves regulation of the actin cytoskeleton. Mol. Cell. Biol. 14, 4193–4202 (1994).
  Article CAS Google Scholar
• Liu, A.-X., Du, W., Liu, J.-P., Jessell, T. M. & Prendergast, G. C. RhoB alteration is required for the apoptotic and antineoplastic responses to farnesyltransferase inhibitors. Mol. Cell. Biol. 20, 6105–6113 (2000).
  Article CAS Google Scholar
• Kohl, N. E. et al. Inhibition of farnesyltransferase induces regression of mammary and salivary carcinomas in ras transgenic mice. Nature Med. 1, 792–797 (1995).
  Article CAS Google Scholar
• Fritz, G. & Kaina, B. RhoB encoding a UV-inducible ras-related small GTP-binding protein is regulated by GTPases of the rho family and independent of JNK, ERK, and p38 MAP kinase. J. Biol. Chem. 272, 30637–30644 (1997).
  Article CAS Google Scholar
• Liu, A.-X., Cerniglia, G. J., Bernhard, E. J. & Prendergast, G. C. RhoB is required for the apoptotic response of neoplastically transformed cells to DNA damage. Proc. Natl Acad. Sci. USA 98, 6192–6197 (2001).
  Article Google Scholar
• Lowe, S. W., Ruley, H. E., Jacks, T. & Housman, D. E. p53-dependent apoptosis modulates the cytotoxicity of anticancer agents. Cell 74, 957–967 (1993).
  Article CAS Google Scholar
• Bernhard, E. J. et al. The farnesyltransferase inhibitor FTI-277 radiosensitizes Hras-transformed rat embryo fibroblasts. Cancer Res. 56, 1727–1730 (1996).
  CAS PubMed Google Scholar
• Bernhard, E. J. et al. Inhibiting Ras prenylation increases the radiosensitivity of human tumor cell lines with activating mutations of Ras oncogenes. Cancer Res. 58, 1754–1761 (1998).
  CAS PubMed Google Scholar
• Fritz, G. & Kaina, B. Ras-related GTPase RhoB forces alkylation-induced apoptotic cell death. Biochem. Biophys. Res. Comm. 268, 784–789 (2000).
  Article CAS Google Scholar
• Mendrysa, S. M. & Perry, M. E. The p53 tumor suppressor protein does regulate expression of its own inhibitor, MDM2, except under conditions of stress. Mol. Cell. Biol. 20, 2023–2030 (2000).
  Article CAS Google Scholar
• Liu, J. P. & Jessell, T. M. A role for RhoB in the delamination of neural crest cells from the dorsal neural tube. Development 125, 5055–5067 (1998).
  CAS PubMed Google Scholar
• Flynn, P., Mellor, H., Casamassima, A. & Parker, P. J. Rho GTPase control of protein kinase C-related protein kinase activation by 3-phosphoinositide-dependent protein kinase. J. Biol. Chem. 275, 11064–11070 (2000).
  Article CAS Google Scholar
• Balendran, A. et al. PDK1 acquires PDK2 activity in the presence of a synthetic peptide derived from the carboxyl terminus of PRK2. Curr. Biol. 9, 393–404 (1999).
  Article CAS Google Scholar
• Jiang, K. et al. The phosphoinositide 3-OH kinase/AKT2 pathway as a critical target for farnesyltransferase inhibitor-induced apoptosis. Mol. Cell. Biol. 20, 139–148 (2000).
  Article Google Scholar
• Liu, A.-X. & Prendergast, G. C. Geranylgeranylated RhoB is sufficient to mediate tissue-specific suppression of Akt kinase activity by farnesyltransferase inhibitors. FEBS Lett. 481, 205–208 (2000).
  Article CAS Google Scholar
• Du, W., Liu, A. & Prendergast, G. C. Activation of the PI3K–AKT pathway masks the proapoptotic effect of farnesyltransferase inhibitors. Cancer Res. 59, 4808–4812 (1999).
  Google Scholar
• Fritz, G. & Kaina, B. Ras-related GTPase RhoB represses NF-κB signaling. J. Biol. Chem. 276, 3115–3122 (2001).
  Article CAS Google Scholar
• Montaner, S., Perona, R., Saniger, L. & Lacal, J. C. Multiple signalling pathways lead to the activation of the nuclear factor-αB by the Rho family of GTPases. J. Biol. Chem. 273, 12779–12785 (1998).
  Article CAS Google Scholar
• Perona, R. et al. Activation of the nuclear factor-κB by Rho, Cdc42, and Rac-1 proteins. Genes Dev. 11, 463–475 (1997).
  Article CAS Google Scholar
• Gnad, R., Kaina, B. & Fritz, G. Rho GTPases are involved in the regulation of NF-κB by genotoxic stress. Exp. Cell Res. 264, 244–249 (2001).
  Article CAS Google Scholar
• Kato, T. et al. Localization of a mammalian homolog of diaphanous, mDia1, to the mitotic spindle in HeLa cells. J. Cell Sci. 114, 775–784 (2001).
  CAS PubMed Google Scholar
• Miquel, K. et al. GGTI-298 induces G0-G1 block and apoptosis whereas FTI-277 causes G2-M enrichment in A549 cells. Cancer Res. 57, 1846–1850 (1997).
  CAS PubMed Google Scholar
• Song, S. Y., Meszoely, I. M., Coffey, R. J., Pietenpol, J. A. & Leach, S. D. KRas-independent effects of the farnesyl transferase inhibitor L-744,832 on cyclin B1/cdc2 kinase activity, G2/M cell cycle progression and apoptosis in human pancreatic ductal adenocarcinoma cells. Neoplasia 2, 261–272 (2000).
  Article CAS Google Scholar
• Ashar, H. R. et al. The farnesyl transferase inhibitor SCH 66336 induces a G2 → M or G1 pause in sensitive human tumor cell lines. Exp. Cell Res. 262, 17–27 (2001).
  Article CAS Google Scholar
• Crespo, N. C., Ohkanda, J., Yen, T. J., Hamilton, A. D. & Sebti, S. M. The farnesyltransferase inhibitor, FTI-2153, blocks bipolar spindle formation and chromosome alignment and causes prometaphase accumulation during mitosis of human lung cancer cells. J. Biol. Chem. 276, 16161–16167 (2001).
  Article CAS Google Scholar
• Gachet, Y., Tournier, S., Millar, J. B. A. & Hyams, J. S. A MAP kinase-dependent actin checkpoint ensures proper spindle orientation in fission yeast. Nature 412, 352–354 (2001).
  Article CAS Google Scholar
• Fritz, G. & Kaina, B. Transcriptional activation of the small GTPase gene RhoB by genotoxic stress is regulated via a CCAAT element. Nucleic Acids Res. 29, 792–798 (2001).
  Article CAS Google Scholar
• Prendergast, G. C. Mode of action of farnesyltransferase inhibitors. Lancet Oncology 1, 73 (2000).
  Article CAS Google Scholar
• Clark, E. A., Golub, T. R., Lander, E. S. & Hynes, R. O. Genomic analysis of metastasis reveals an essential role for RhoC. Nature 406, 532–535 (2000).
  Article CAS Google Scholar
• Ise, K. et al. Targeted deletion of the Hras gene decreases tumor formation in mouse skin carcinogenesis. Oncogene 19, 2951–2956 (2000).
  Article CAS Google Scholar
• Suwa, H. et al. Overexpression of the RhoC gene correlates with progression of ductal adenocarcinoma of the pancreas. Br. J. Cancer 77, 147–152 (1998).
  Article CAS Google Scholar
• van Golen, K. L. et al. A novel putative low-affinity insulin-like growth factor-binding protein, LIBC (lost in inflammatory breast cancer), and RhoC GTPase correlate with the inflammatory breast cancer phenotype. Clin. Cancer Res. 5, 2511–2519 (1999).
  CAS PubMed Google Scholar