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RHO-GTPases and cancer

Sahai, Erik, Marshall, Christopher J.·2002·Nature Reviews Cancer

Abstract

The RAS oncogenes were identified almost 20 years ago. Since then, we have learnt that they are members of a large family of small GTPases that bind GTP and hydrolyse it to GDP. This is then exchanged for GTP and the cycle is repeated. The switching between these two states regulates a wide range of cellular processes. A branch of the RAS family--the RHO proteins--is also involved in cancer, but what is the role of these proteins and would they make good therapeutic targets?

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  1. Lander, E. S. et al. Initial sequencing and analysis of the human genome. Nature 409, 860–921 (2001). · DOI · Paper page
  2. Bishop, A. L. & Hall, A. Rho GTPases and their effector proteins. Biochem. J. 348, 241–255 (2000). · DOI · Paper page
  3. Hall, A. Rho GTPases and the actin cytoskeleton. Science 279, 509–514 (1998). · DOI
  4. Van Aelst, L. & D'Souza-Schorey, C. Rho GTPases and signaling networks. Genes Dev. 11, 2295–2322 (1997). · DOI
  5. Qiu, R. G., Chen, J., McCormick, F. & Symons, M. A role for Rho in Ras transformation. Proc. Natl Acad. Sci. USA 92, 11781–11785 (1995). One of the first reports to indicate involvement of a RHO-family member in RAS-mediated transformation (see also references 6 , and 10). · DOI · Paper page
  6. Qiu, R. G., Chen, J., Kirn, D., McCormick, F. & Symons, M. An essential role for Rac in Ras transformation. Nature 374, 457–459 (1995). · DOI
  7. Qiu, R. G., Abo, A., McCormick, F. & Symons, M. Cdc42 regulates anchorage-independent growth and is necessary for Ras transformation. Mol. Cell Biol. 17, 3449–3458 (1997). · DOI
  8. Roux, P., Gauthier-Rouviere, C., Doucet-Brutin, S. & Fort, P. The small GTPases Cdc42Hs, Rac1 and RhoG delineate Raf-independent pathways that cooperate to transform NIH3T3 cells. Curr. Biol. 7, 629–637 (1997). · DOI
  9. Murphy, G. A. et al. Cellular functions of TC10, a Rho family GTPase: regulation of morphology, signal transduction and cell growth. Oncogene 18, 3831–3845 (1999). · DOI
  10. Khosravi-Far, R., Solski, P. A., Clark, G. J., Kinch, M. S. & Der, C. J. Activation of Rac1, RhoA, and mitogen-activated protein kinases is required for Ras transformation. Mol. Cell Biol. 15, 6443–6453 (1995). · DOI · Paper page
  11. Ingram, D. A. et al. Hyperactivation of p21(Ras) and the hematopoietic-specific Rho GTPase, Rac2, cooperate to alter the proliferation of neurofibromin-deficient mast cells in vivo and in vitro. J. Exp. Med. 194, 57–69 (2001). Genetic manipulation of mice shows the importance of Rac2 in proliferation of mast cells with hyperactive Ras. · DOI
  12. Kourlas, P. J. et al. Identification of a gene at 11q23 encoding a guanine nucleotide exchange factor: evidence for its fusion with MLL in acute myeloid leukemia. Proc. Natl Acad. Sci. USA 97, 2145–2150 (2000). · DOI
  13. Kin, Y., Li, G., Shibuya, M. & Maru, Y. The DBL homology domain of BCR is not a simple spacer in p210 BCR–ABL of the Philadelphia chromosome. J. Biol. Chem. 276, 39462–39468 (2001). · DOI
  14. Reuther, G. W. et al. Leukemia-associated Rho guanine nucleotide exchange factor, a Dbl family protein found mutated in leukemia, causes transformation by activation of RhoA. J. Biol. Chem. 276, 27145–27151 (2001). · DOI
  15. Preudhomme, C. et al. Nonrandom 4p13 rearrangements of the RhoH/TTF gene, encoding a GTP-binding protein, in non-Hodgkin's lymphoma and multiple myeloma. Oncogene 19, 2023–2032 (2000). · DOI · Paper page
  16. Pasqualucci, L. et al. Hypermutation of multiple proto-oncogenes in B-cell diffuse large-cell lymphomas. Nature 412, 341–346 (2001). · DOI · Paper page
  17. Kamai, T., Arai, K., Tsujii, T., Honda, M. & Yoshida, K. Overexpression of RhoA mRNA is associated with advanced stage in testicular germ cell tumour. BJU Int. 87, 227–231 (2001). · DOI
  18. Fritz, G., Just, I. & Kaina, B. Rho GTPases are over-expressed in human tumors. Int. J. Cancer 81, 682–687 (1999). · DOI
  19. 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). · DOI · Paper page
  20. van Golen, K. L., Wu, Z. F., Qiao, X. T., Bao, L. W. & Merajver, 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).
  21. Schnelzer, A. et al. Rac1 in human breast cancer: overexpression, mutation analysis, and characterization of a new isoform, Rac1b. Oncogene 19, 3013–3020 (2000). Intriguing paper showing that the splice variant of RAC1 that is highly expressed in breast and colon cancer has an increased GDP–GTP exchange rate (see also reference 22 ). An increased GDP–GTP exchange rate can promote transformation of fibroblasts (see reference 33). · DOI · Paper page
  22. Jordan, P., Brazao, R., Boavida, M. G., Gespach, C. & Chastre, E. Cloning of a novel human Rac1b splice variant with increased expression in colorectal tumors. Oncogene 18, 6835–6839 (1999). · DOI
  23. Zondag, G. C. et al. Oncogenic Ras downregulates Rac activity, which leads to increased Rho activity and epithelial-mesenchymal transition. J. Cell Biol. 149, 775–782 (2000). · DOI
  24. Royal, I., Lamarche-Vane, N., Lamorte, L., Kaibuchi, K. & Park, M. Activation of CDC42, RAC, PAK, and Rho-kinase in response to hepatocyte growth factor differentially regulates epithelial cell colony spreading and dissociation. Mol. Biol. Cell 11, 1709–1725 (2000). · DOI
  25. Fukata, M. et al. Involvement of IQGAP1, an effector of Rac1 and Cdc42 GTPases, in cell–cell dissociation during cell scattering. Mol. Cell. Biol. 21, 2165–2183 (2001). · DOI
  26. Bhowmick, N. A. et al. Transforming growth factor-β1 mediates epithelial to mesenchymal transdifferentiation through a RhoA-dependent mechanism. Mol. Biol. Cell 12, 27–36 (2001). · DOI
  27. 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). · DOI
  28. Habas, R., Kato, Y. & He, X. Wnt/Frizzled activation of Rho regulates vertebrate gastrulation and requires a novel formin homology protein Daam1. Cell 107, 843–854 (2001). · DOI · Paper page
  29. Kawasaki, Y. et al. Asef, a link between the tumor suppressor APC and G-protein signaling. Science 289, 1194–1197 (2000). · DOI
  30. Tao, W., Pennica, D., Xu, L., Kalejta, R. F. & Levine, A. J. Wrch-1, a novel member of the Rho gene family that is regulated by Wnt-1. Genes Dev. 15, 1796–1807 (2001). · DOI
  31. Baron, M., O'Leary, V., Evans, D. A., Hicks, M. & Hudson, K. Multiple roles of the Dcdc42 GTPase during wing development in Drosophila melanogaster . Mol Gen Genet 264, 98–104 (2000). · DOI
  32. Winter, C. G. et al. Drosophila Rho-associated kinase (Drok) links Frizzled-mediated planar cell polarity signaling to the actin cytoskeleton. Cell 105, 81–91 (2001). · DOI
  33. Lin, R., Bagrodia, S., Cerione, R. & Manor, D. A novel Cdc42Hs mutant induces cellular transformation. Curr. Biol. 7, 794–797 (1997). · DOI
  34. Ridley, A. J., Paterson, H. F., Johnston, C. L., Diekmann, D. & Hall, A. The small GTP-binding protein RAC regulates growth factor-induced membrane ruffling. Cell 70, 401–410 (1992). · DOI
  35. Nobes, C. D. & Hall, A. Rho, RAC, and CDC42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia. Cell 81, 53–62 (1995). · DOI
  36. Sahai, E., Olson, M. F. & Marshall, C. J. Cross-talk between Ras and Rho signalling pathways in transformation favours proliferation and increased motility. EMBO J. 20, 755–766 (2001). · DOI
  37. Mira, J. P., Benard, V., Groffen, J., Sanders, L. C. & Knaus, U. G. Endogenous, hyperactive Rac3 controls proliferation of breast cancer cells by a p21-activated kinase-dependent pathway. Proc. Natl Acad. Sci. USA 97, 185–189 (2000). · DOI
  38. 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). RHOC is required in vivo for the metastasis of melanoma cells. RHOC mRNA is upregulated in melanoma cell lines that are selected for high metastatic potential. · DOI
  39. Ridley, A. J. Rho GTPases and cell migration. J. Cell Sci. 114, 2713–2722 (2001). · DOI
  40. Itoh, K. et al. An essential part for Rho-associated kinase in the transcellular invasion of tumor cells. Nature Med. 5, 221–225 (1999). RHOA–ROCK signalling can promote dissemination of tumour cells, and this can be blocked using a pharmacological inhibitor of ROCK in vivo. · DOI
  41. Murata, T. et al. Inhibitory effect of Y-27632, a ROCK inhibitor, on progression of rat liver fibrosis in association with inactivation of hepatic stellate cells. J. Hepatol. 35, 474–481 (2001). · DOI
  42. Somlyo, A. V. et al. Rho-kinase inhibitor retards migration and in vivo dissemination of human prostate cancer cells. Biochem. Biophys. Res. Commun. 269, 652–659 (2000). · DOI
  43. Guasch, R. M., Scambler, P., Jones, G. E. & Ridley, A. J. RhoE regulates actin cytoskeleton organization and cell migration. Mol. Cell. Biol. 18, 4761–4771 (1998). · DOI · Paper page
  44. Nobes, C. D. et al. A new member of the Rho family, Rnd1, promotes disassembly of actin filament structures and loss of cell adhesion. J. Cell Biol. 141, 187–197 (1998). · DOI
  45. Hansen, S. H. et al. Induced expression of Rnd3 is associated with transformation of polarized epithelial cells by the Raf–MEK–extracellular signal-regulated kinase pathway. Mol. Cell. Biol. 20, 9364–9375 (2000). · DOI · Paper page
  46. O'Brien, L. E. et al. Rac1 orientates epithelial apical polarity through effects on basolateral laminin assembly. Nature Cell Biol. 3, 831–838 (2001). · DOI
  47. Kim, S. K. Cell polarity: new PARtners for Cdc42 and Rac. Nature Cell Biol. 2, E143–E145 (2000). · DOI
  48. Braga, V. M., Betson, M., Li, X. & Lamarche-Vane, N. Activation of the small GTPase Rac is sufficient to disrupt cadherin-dependent cell–cell adhesion in normal human keratinocytes. Mol. Biol. Cell 11, 3703–3721 (2000). · DOI
  49. Quinlan, M. P. Rac regulates the stability of the adherens junction and its components, thus affecting epithelial cell differentiation and transformation. Oncogene 18, 6434–6442 (1999). · DOI
  50. Sander, E. E. et al. Matrix-dependent Tiam1/Rac signaling in epithelial cells promotes either cell–cell adhesion or cell migration and is regulated by phosphatidylinositol 3-kinase. J. Cell Biol. 143, 1385–1398 (1998). · DOI
  51. Matsui, T. et al. Rho-kinase phosphorylates COOH-terminal threonines of ezrin/radixin/moesin (ERM) proteins and regulates their head-to-tail association. J. Cell Biol. 140, 647–657 (1998). · DOI
  52. Shaw, R. J. et al. The Nf2 tumor suppressor, merlin, functions in Rac-dependent signaling. Dev. Cell 1, 63–72 (2001).Shows how a link between RAC and the tumour suppressor NF2 might promote proliferation and cell motility. This link might be important in tumorigenesis (see also reference 58). · DOI
  53. Xiao, G. H., Beeser, A., Chernoff, J. & Testa, J. R. p21-activated kinase links Rac/Cdc42 signaling to Merlin. J. Biol. Chem. 21, 21 (2001).
  54. Khanna, C. et al. Metastasis-associated differences in gene expression in a murine model of osteosarcoma. Cancer Res. 61, 3750–3759 (2001).
  55. Akisawa, N., Nishimori, I., Iwamura, T., Onishi, S. & Hollingsworth, M. A. High levels of ezrin expressed by human pancreatic adenocarcinoma cell lines with high metastatic potential. Biochem. Biophys. Res. Commun. 258, 395–400 (1999). · DOI
  56. Clarke, G., Ryan, E., O'Keane, J. C., Crowe, J. & Mathuna, P. M. Mortality association of enhanced CD44v6 expression is not mediated through occult lymphatic spread in stage II colorectal cancer. J. Gastroenterol. Hepatol. 15, 1028–1031 (2000). · DOI
  57. Harada, N. et al. Introduction of antisense CD44S cDNA down-regulates expression of overall CD44 isoforms and inhibits tumor growth and metastasis in highly metastatic colon carcinoma cells. Int. J. Cancer 91, 67–75 (2001). · DOI
  58. McClatchey, A. I. et al. Mice heterozygous for a mutation at the Nf2 tumor suppressor locus develop a range of highly metastatic tumors. Genes Dev. 12, 1121–1133 (1998). · DOI
  59. Zhuge, Y. & Xu, J. Rac1 mediates type I collagen-dependent MMP-2 activation: role in cell invasion across collagen barrier. J. Biol. Chem. 276, 16248–16256 (2001). · DOI
  60. Engers, R., Springer, E., Michiels, F., Collard, J. G. & Gabbert, H. E. Rac affects invasion of human renal cell carcinomas by upregulating TIMP-1 and TIMP-2 expression. J. Biol. Chem. 276, 41889–41897(2001). · DOI
  61. Kheradmand, F., Werner, E., Tremble, P., Symons, M. & Werb, Z. Role of Rac1 and oxygen radicals in collagenase-1 expression induced by cell shape change. Science 280, 898–902 (1998). · DOI
  62. Matsumoto, Y. et al. Small GTP-binding protein, Rho, both increased and decreased cellular motility, activation of matrix metalloproteinase 2 and invasion of human osteosarcoma cells. Jpn. J. Cancer Res. 92, 429–438 (2001). · DOI
  63. Worthylake, R. A., Lemoine, S., Watson, J. M. & Burridge, K. RhoA is required for monocyte tail retraction during transendothelial migration. J. Cell Biol. 154, 147–160 (2001). · DOI
  64. Adamson, P., Etienne, S., Couraud, P. O., Calder, V. & Greenwood, J. Lymphocyte migration through brain endothelial cell monolayers involves signaling through endothelial ICAM-1 via a Rho-dependent pathway. J. Immunol. 162, 2964–2973 (1999). · DOI
  65. van Golen, K. L., Wu, Z. F., Qiao, X. T., Bao, L. & Merajver, S. D. RhoC GTPase overexpression modulates induction of angiogenic factors in breast cells. Neoplasia 2, 418–425 (2000). · DOI
  66. Soede, R. D. M. et al. Stromal cell-derived factor-1-induced LFA-1 activation during in vivo migration of T cell hybridoma cells requires Gq/11, RhoA, and myosin, as well as Gi and Cdc42. J. Immunol. 166, 4293–4301 (2001). · DOI
  67. Pines, J. The cell cycle kinases. Semin. Cancer Biol. 5, 305–313 (1994).
  68. Sherr, C. J. & Roberts, J. M. CDK inhibitors: positive and negative regulators of G1-phase progression. Genes Dev. 13, 1501–1512 (1999). · DOI · Paper page
  69. Robles, A. I. et al. Reduced skin tumor development in cyclin D1-deficient mice highlights the oncogenic Ras pathway in vivo. Genes Dev. 12, 2469–2474 (1998). · DOI
  70. Shaulian, E. & Karin, M. AP-1 in cell proliferation and survival. Oncogene 20, 2390–2400 (2001). · DOI
  71. Albanese, C. et al. Transforming p21Ras mutants and c-Ets-2 activate the cyclin D1 promoter through distinguishable regions. J. Biol. Chem. 270, 23589–23597 (1995). · DOI
  72. Hinz, M. et al. NF-κB function in growth control: regulation of cyclin D1 expression and G0/G1-to-S-phase transition. Mol. Cell. Biol. 19, 2690–2698 (1999). · DOI
  73. Vojtek, A. B. & Cooper, J. A. Rho family members: activators of MAP kinase cascades. Cell 82, 527–529 (1995). · DOI · Paper page
  74. Westwick, J. K. et al. Rac regulation of transformation, gene expression, and actin organization by multiple, PAK-independent pathways. Mol. Cell. Biol. 17, 1324–1335 (1997). · DOI
  75. Marinissen, M. J., Chiariello, M. & Gutkind, J. S. Regulation of gene expression by the small GTPase Rho through the ERK6 (p38-γ) MAP kinase pathway. Genes Dev. 15, 535–553 (2001). · DOI
  76. Hill, C. S., Wynne, J. & Treisman, R. The Rho family GTPases RhoA, Rac1, and CDC42Hs regulate transcriptional activation by SRF. Cell 81, 1159–1170 (1995). · DOI
  77. Benbow, U. & Brinckerhoff, C. E. The AP-1 site and MMP gene regulation: what is all the fuss about? Matrix Biol. 15, 519–526 (1997). · DOI
  78. Frost, J. A. et al. Cross-cascade activation of ERKs and ternary complex factors by Rho family proteins. EMBO J. 16, 6426–6438 (1997). · DOI
  79. Welsh, C. F. et al. Timing of cyclin D1 expression within G1 phase is controlled by Rho. Nature Cell Biol. 3, 950–957 (2001). · DOI
  80. King, A. J. et al. The protein kinase Pak3 positively regulates Raf-1 activity through phosphorylation of serine 338. Nature 396, 180–183 (1998). · DOI
  81. Narumiya, S., Ishizaki, T. & Watanabe, N. Rho effectors and reorganization of actin cytoskeleton. FEBS Lett. 410, 68–72 (1997). · DOI
  82. Danen, E. H. & Yamada, K. M. Fibronectin, integrins, and growth control. J. Cell Physiol. 189, 1–13 (2001). · DOI
  83. Assoian, R. K. & Schwartz, M. A. Coordinate signaling by integrins and receptor tyrosine kinases in the regulation of G1 phase cell-cycle progression. Curr. Opin. Genet. Dev. 11, 48–53 (2001). · DOI
  84. Joneson, T. & Bar-Sagi, D. Suppression of Ras-induced apoptosis by the Rac GTPase. Mol. Cell. Biol. 19, 5892–5901 (1999). · DOI
  85. Joyce, D. et al. Integration of Rac-dependent regulation of cyclin D1 transcription through a nuclear factor-κB-dependent pathway. J. Biol. Chem. 274, 25245–25249 (1999). · DOI
  86. Cammarano, M. S. & Minden, A. Dbl and the Rho GTPases activate NFκB by IκB kinase (IKK)-dependent and IKK-independent pathways. J. Biol. Chem. 276, 25876–25882 (2001). · DOI
  87. Frost, J. A. et al. Stimulation of NFκB activity by multiple signaling pathways requires PAK1. J. Biol. Chem. 275, 19693–19699 (2000). · DOI
  88. Lallena, M. J., Diaz-Meco, M. T., Bren, G., Paya, C. V. & Moscat, J. Activation of IκB kinase-β by protein kinase C isoforms. Mol. Cell. Biol. 19, 2180–2188 (1999). · DOI
  89. Qiu, R. G., Abo, A. & Steven Martin, G. A human homolog of the C. elegans polarity determinant Par-6 links Rac and Cdc42 to PKCζ signaling and cell transformation. Curr. Biol. 10, 697–707 (2000). · DOI
  90. Murphy, G. A. et al. Signaling mediated by the closely related mammalian Rho family GTPases TC10 and Cdc42 suggests distinct functional pathways. Cell Growth Differ. 12, 157–167 (2001).
  91. Sonenshein, G. E. Rel/NF-κB transcription factors and the control of apoptosis. Semin. Cancer Biol. 8, 113–119 (1997). · DOI
  92. Mettouchi, A. et al. Integrin-specific activation of Rac controls progression through the G(1) phase of the cell cycle. Mol. Cell 8, 115–127 (2001).RAC1 acts downstream of a physical cue — integrin engagement — to upregulate cyclin D1 in a transcription-independent manner. · DOI
  93. Olson, M. F., Paterson, H. F. & Marshall, C. J. Signals from Ras and Rho GTPases interact to regulate expression of p21Waf1/Cip1. Nature 394, 295–299 (1998). A crucial link between RHOA and the cell-cycle regulator p21WAF1 is demonstrated in the context of oncogenic RAS signalling (see also reference 112). · DOI
  94. Sahai, E., Ishizaki, T., Narumiya, S. & Treisman, R. Transformation mediated by RhoA requires activity of ROCK kinases. Curr. Biol. 9, 136–145 (1999). · DOI
  95. Tran Quang, C., Gautreau, A., Arpin, M. & Treisman, R. Ezrin function is required for ROCK-mediated fibroblast transformation by the Net and Dbl oncogenes. EMBO J. 19, 4565–4576 (2000). · DOI
  96. Adnane, J., Bizouarn, F. A., Qian, Y., Hamilton, A. D. & Sebti, S. M. p21(WAF1/CIP1) is upregulated by the geranylgeranyltransferase I inhibitor GGTI-298 through a transforming growth factor-β- and Sp1-responsive element: involvement of the small GTPase RhoA. Mol. Cell. Biol. 18, 6962–6970 (1998). · DOI
  97. Hirai, A. et al. Geranylgeranylated rho small GTPase(s) are essential for the degradation of p27Kip1 and facilitate the progression from G1 to S phase in growth-stimulated rat FRTL-5 cells. J. Biol. Chem. 272, 13–16 (1997). · DOI
  98. Weber, J. D., Hu, W., Jefcoat, S. C. Jr, Raben, D. M. & Baldassare, J. J. Ras-stimulated extracellular signal-related kinase 1 and RhoA activities coordinate platelet-derived growth factor-induced G1 progression through the independent regulation of cyclin D1 and p27. J. Biol. Chem. 272, 32966–32971 (1997). · DOI
  99. Tanaka, T. et al. Activation of cyclin-dependent kinase 2 (Cdk2) in growth-stimulated rat astrocytes. Geranylgeranylated Rho small GTPase(s) are essential for the induction of cyclin E gene expression. J. Biol. Chem. 273, 26772–26778 (1998). · DOI
  100. Ghosh, P. M., Moyer, M. L., Mott, G. E. & Kreisberg, J. I. Effect of cyclin E overexpression on lovastatin-induced G1 arrest and RhoA inactivation in NIH3T3 cells. J. Cell Biochem. 74, 532–543 (1999). · DOI
  101. Chiariello, M., Marinissen, M. J. & Gutkind, J. S. Regulation of c-myc expression by PDGF through Rho GTPases. Nature Cell Biol. 3, 580–586 (2001). · DOI
  102. 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). · DOI
  103. Wu, W. J., Erickson, J. W., Lin, R. & Cerione, R. A. The γ-subunit of the coatomer complex binds Cdc42 to mediate transformation. Nature 405, 800–804 (2000). · DOI
  104. Lamaze, C., Chuang, T. H., Terlecky, L. J., Bokoch, G. M. & Schmid, S. L. Regulation of receptor-mediated endocytosis by Rho and Rac. Nature 382, 177–179 (1996). · DOI
  105. Murphy, C. et al. Endosome dynamics regulated by a Rho protein. Nature 384, 427–432 (1996). · DOI
  106. Malecz, N. et al. Synaptojanin 2, a novel Rac1 effector that regulates clathrin-mediated endocytosis. Curr. Biol. 10, 1383–1386 (2000). · DOI
  107. Hotta, K., Tanaka, K., Mino, A., Kohno, H. & Takai, Y. Interaction of the Rho family small G proteins with kinectin, an anchoring protein of kinesin motor. Biochem. Biophys. Res. Commun. 225, 69–74 (1996). · DOI
  108. Vignal, E., Blangy, A., Martin, M., Gauthier-Rouviere, C. & Fort, P. Kinectin is a key effector of RhoG microtubule-dependent cellular activity. Mol. Cell. Biol. 21, 8022–8034 (2001). · DOI
  109. Gachet, Y., Tournier, S., Millar, J. B. & Hyams, J. S. A MAP kinase-dependent actin checkpoint ensures proper spindle orientation in fission yeast. Nature 412, 352–355 (2001). · DOI
  110. Ren, X. D., Kiosses, W. B. & Schwartz, M. A. Regulation of the small GTP-binding protein Rho by cell adhesion and the cytoskeleton. EMBO J. 18, 578–585 (1999). · DOI
  111. Noren, N. K., Niessen, C. M., Gumbiner, B. M. & Burridge, K. Cadherin engagement regulates Rho family GTPases. J. Biol. Chem. 16, 16 (2001). · DOI
  112. Danen, E. H., Sonneveld, P., Sonnenberg, A. & Yamada, K. M. Dual stimulation of Ras/mitogen-activated protein kinase and RhoA by cell adhesion to fibronectin supports growth factor-stimulated cell cycle progression. J. Cell Biol. 151, 1413–1422 (2000). RHOA acts downstream of a physical cue — integrin engagement — to downregulate p21WAF1 and promote proliferation (see also reference 93). · DOI
  113. Coleman, M. L. & Olson, M. F. Rho GTPase signalling pathways in the morphological changes associated with apoptosis. Cell Death Differ. (in the press). · DOI
  114. Pervaiz, S., Cao, J., Chao, O. S., Chin, Y. Y. & Clement, M. V. Activation of the RacGTPase inhibits apoptosis in human tumor cells. Oncogene 20, 6263–6268 (2001). · DOI
  115. Coniglio, S. J., Jou, T. S. & Symons, M. Rac1 protects epithelial cells against anoikis. J. Biol. Chem. 276, 28113–28120 (2001). · DOI
  116. Tang, Y., Zhou, H., Chen, A., Pittman, R. N. & Field, J. The Akt proto-oncogene links Ras to Pak and cell survival signals. J. Biol. Chem. 275, 9106–9109 (2000). · DOI
  117. Schurmann, A. et al. p21-activated kinase 1 phosphorylates the death agonist bad and protects cells from apoptosis. Mol. Cell. Biol. 20, 453–461 (2000). · DOI
  118. Yang, F. C. et al. Rac2 stimulates Akt activation affecting BAD/BCL-XL expression while mediating survival and actin function in primary mast cells. Immunity 12, 557–568 (2000). · DOI · Paper page
  119. Costello, P. S., Cleverley, S. C., Galandrini, R., Henning, S. W. & Cantrell, D. A. The GTPase Rho controls a p53-dependent survival checkpoint during thymopoiesis. J. Exp. Med. 192, 77–85 (2000). · DOI
  120. Liu, A., Cerniglia, G. J., Bernhard, E. J. & Prendergast, G. C. RhoB is required to mediate apoptosis in neoplastically transformed cells after DNA damage. Proc. Natl Acad. Sci. USA 98, 6192–6197 (2001). · DOI
  121. Prendergast, G. C. Actin' up: RhoB in cancer and apoptosis. Nature Rev. Cancer 1, 162–168 (2001). · DOI
  122. Subauste, M. C. et al. Rho family proteins modulate rapid apoptosis induced by cytotoxic T lymphocytes and Fas. J. Biol. Chem. 275, 9725–9733 (2000). · DOI
  123. Brenner, B. et al. Fas- or ceramide-induced apoptosis is mediated by a Rac1-regulated activation of Jun N-terminal kinase/p38 kinases and GADD153. J. Biol. Chem. 272, 22173–22181 (1997). · DOI
  124. Sebti, S. M. & Hamilton, A. D. Inhibition of Rho GTPases using protein geranylgeranyltransferase I inhibitors. Methods Enzymol. 325, 381–388 (2000). · DOI
  125. Vastrik, I., Eickholt, B. J., Walsh, F. S., Ridley, A. & Doherty, P. Sema3A-induced growth-cone collapse is mediated by Rac1 amino acids 17–32. Curr. Biol. 9, 991–998 (1999). · DOI
  126. Chardin, P. & McCormick, F. Brefeldin A: the advantage of being uncompetitive. Cell 97, 153–155 (1999). · DOI · Paper page
  127. Du, W. & Prendergast, G. C. Geranylgeranylated RhoB mediates suppression of human tumor cell growth by farnesyltransferase inhibitors. Cancer Res. 59, 5492–5496 (1999).
  128. Liu, A., Du, W., Liu, J. P., Jessell, T. M. & Prendergast, G. C. RhoB alteration is necessary for apoptotic and antineoplastic responses to farnesyltransferase inhibitors. Mol. Cell. Biol. 20, 6105–6113 (2000). · DOI
  129. Pollack, I. F., Bredel, M., Erff, M., Hamilton, A. D. & Sebti, S. M. Inhibition of Ras and related guanosine triphosphate-dependent proteins as a therapeutic strategy for blocking malignant glioma growth: II. Preclinical studies in a nude mouse model. Neurosurgery 45, 1208–1214; discussion 1214–1205 (1999). · DOI
  130. Sun, J., Qian, Y., Hamilton, A. D. & Sebti, S. M. Both farnesyltransferase and geranylgeranyltransferase I inhibitors are required for inhibition of oncogenic K-Ras prenylation but each alone is sufficient to suppress human tumor growth in nude mouse xenografts. Oncogene 16, 1467–1473 (1998). · DOI
  131. Ishizaki, T. et al. Coordination of microtubules and the actin cytoskeleton by the Rho effector mDia1. Nature Cell Biol. 3, 8–14 (2001). · DOI
  132. Ellis, S. & Mellor, H. The novel Rho-family GTPase rif regulates coordinated actin-based membrane rearrangements. Curr. Biol. 10, 1387–1390 (2000). · DOI
  133. Aronheim, A. et al. Chp, a homologue of the GTPase Cdc42Hs, activates the JNK pathway and is implicated in reorganizing the actin cytoskeleton. Curr. Biol. 8, 1125–1128 (1998). · DOI
  134. Vignal, E. et al. Characterization of TCL, a new GTPase of the Rho family related to TC10 and Cdc42. J. Biol. Chem. 275, 36457–36464 (2000). · DOI
  135. Neudauer, C. L., Joberty, G. & Macara, I. G. PIST: a novel PDZ/coiled-coil domain binding partner for the Rho-family GTPase TC10. Biochem. Biophys. Res. Commun. 280, 541–547 (2001). · DOI
  136. Chiang, S. H. et al. Insulin-stimulated GLUT4 translocation requires the CAP-dependent activation of TC10. Nature 410, 944–948 (2001). · DOI
  137. Abraham, M. T. et al. Motility-related proteins as markers for head and neck squamous cell cancer. Laryngoscope 111, 1285–1289 (2001). · DOI
  138. 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).
  139. Engers, R. et al. Tiam1 mutations in human renal-cell carcinomas. Int. J. Cancer 88, 369–376 (2000). · DOI

Cited by

Metadata

Authors
Sahai, E., & Marshall, C. J.
Venue
Nature Reviews Cancer
Published
2002-02
Volume
2
Issue
2
Pages
133-142
ISSN
  • 1474-175X
  • 1474-1768
Cited by
1,261
References
1
Language
en

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