Raf-1 Physically Interacts with Rb and Regulates Its Function: a Link between Mitogenic Signaling and Cell Cycle Regulation

REFERENCES

• Atkas, H., H. Cai, and G. M. Cooper 1997. Ras links growth factor signaling to the cell cycle machinery via regulation of cyclin D1 and the cdk inhibitor p27 Kip1. Mol. Cell. Biol. 17: 3850–3857.
   PubMedGoogle Scholar
• Bagchi, S., P. Raychaudhuri, and J. R. Nevins 1990. Adenovirus E1A proteins can dissociate heteromeric complexes involving the E2F transcription factor: a novel mechanism for E1A trans-activation. Cell 62: 659–669.
   PubMed Web of Science ®Google Scholar
• Bagchi, S., R. Weinmann, and P. Raychaudhuri 1991. The retinoblastoma protein copurifies with E2F-I, an E1A-regulated inhibitor of the transcription factor E2F. Cell 65: 1073–1082.
   PubMedGoogle Scholar
• Beijersbergen, R. L., and R. Bernards 1996. Cell cycle regulation by the retinoblastoma family of growth inhibitory proteins. Biochim. Biophys. Acta 1287: 103–120.
   PubMed Web of Science ®Google Scholar
• Beijersbergen, R. L., R. M. Kerkhoven, L. Zhu, L. Carlee, P. M. Voorhoeve, and R. Bernards 1994. E2F-4, a new member of the E2F gene family, has oncogenic activity and associates with p107 in vivo. Genes Dev. 8: 2680–2790.
   PubMed Web of Science ®Google Scholar
• Bruder, J. T., G. Heidecker, and U. R. Rapp 1992. Serum-, TPA-, and Ras-induced expression from AP-1/Ets-driven promoters requires Raf-1 kinase. Genes Dev. 6: 545–556.
   PubMedGoogle Scholar
• Buchkovich, K., L. A. Duffy, and E. Harlow 1989. The retinoblastoma protein is phosphorylated during specific phases of the cell cycle. Cell 58: 1097–1105.
   PubMed Web of Science ®Google Scholar
• Burgering, B. M., and J. L. Bos 1995. Regulation of Ras-mediated signalling: more than one way to skin a cat. Trends Biochem. Sci. 20: 18–22.
   PubMed Web of Science ®Google Scholar
• Chellappan, S., V. B. Kraus, B. Kroger, K. Munger, P. M. Howley, W. C. Phelps, and J. R. Nevins 1992. Adenovirus E1A, simian virus 40 tumor antigen, and human papillomavirus E7 protein share the capacity to disrupt the interaction between transcription factor E2F and the retinoblastoma. Proc. Nat. Acad. Sci. USA 89: 4549–4553.
   PubMed Web of Science ®Google Scholar
• Chellappan, S. P., S. Hiebert, M. Mudryj, J. M. Horowitz, and J. R. Nevins 1991. The E2F transcription factor is a cellular target for the RB protein. Cell 65: 1053–1061.
   PubMed Web of Science ®Google Scholar
• Chittenden, T., D. M. Livingston, Kaelin W. G., Jr. 1991. RB associates with an E2F-like, sequence-specific DNA-binding protein. Cold Spring Harbor Symp. Quant. Biol. 56: 187–195.
   PubMedGoogle Scholar
• Claudio, P. P., L. A. De, C. M. Howard, A. Baldi, E. J. Firpo, A. Koff, M. G. Paggi, and A. Giordano 1996. Functional analysis of pRb2/p130 interaction with cyclins. Cancer Res. 56: 2003–2008.
   PubMed Web of Science ®Google Scholar
• Claudio, P. P., C. M. Howard, A. Baldi, L. A. De, Y. Fu, G. Condorelli, Y. Sun, N. Colburn, B. Calabretta, and A. Giordano 1994. p130/pRb2 has growth suppressive properties similar to yet distinctive from those of retinoblastoma family members pRb and p107. Cancer Res. 54: 5556–5560.
   PubMed Web of Science ®Google Scholar
• Cobrinik, D. 1996. Regulatory interactions among E2Fs and cell cycle proteins. Curr. Top. Microbiol. Immunol. 208: 32–63.
   Google Scholar
• Cobrinik, D., P. Whyte, D. S. Peeper, T. Jacks, and R. A. Weinberg 1993. Cell cycle-specific association of E2F with the p130 E1A-binding protein. Genes Dev. 7: 2392–2404.
   PubMed Web of Science ®Google Scholar
• Cox, L. A., G. Chen, and E. Y. Lee 1994. Tumor suppressor genes and their roles in breast cancer. Breast Cancer Res. Treat. 32: 19–38.
   PubMedGoogle Scholar
• Daum, G., I. Eisenmann-Tappe, H. W. Fries, J. Troppmair, and U. R. Rapp 1994. The ins and outs of Raf kinases. Trends Biochem. Sci. 19: 474–479.
   PubMed Web of Science ®Google Scholar
• DeCaprio, J. A., J. W. Ludlow, D. Lynch, Y. Furukawa, J. Griffin, H. Piwnica-Worms, C. M. Huang, and D. M. Livingston 1989. The product of the retinoblastoma susceptibility gene has properties of a cell cycle regulatory element. Cell 58: 1085–1095.
   PubMed Web of Science ®Google Scholar
• DeGregori, J., G. Leone, K. Ohtani, A. Miron, and J. R. Nevins 1995. E2F-1 accumulation bypasses a G1 arrest resulting from the inhibition of G1 cyclin-dependent kinase activity. Genes Dev. 9: 2873–2887.
   PubMed Web of Science ®Google Scholar
• Ewen, M. E., H. K. Sluss, C. J. Sherr, H. Matsushime, J. Kato, and D. M. Livingston 1993. Functional interactions of the retinoblastoma protein with mammalian D-type cyclins. Cell 73: 487–497.
   PubMed Web of Science ®Google Scholar
• Fabian, J. R., I. O. Daar, and D. K. Morrison 1993. Critical tyrosine residues regulate the enzymatic and biological activity of Raf-1 kinase. Mol. Cell. Biol. 13: 7170–7179.
   PubMed Web of Science ®Google Scholar
• Galaktionov, K., C. Jessus, and D. Beach 1995. Raf-1 interaction with Cdc25 phosphatase ties mitogenic signal transduction to cell cycle activation. Genes Dev. 9: 1046–1058.
   PubMed Web of Science ®Google Scholar
• Gautier, J., M. Solomon, R. Booher, J. Bazan, and M. Kirshner 1991. Cdc25 is a specific tyrosine phosphatase that directly activates p34cdc2. Cell 67: 67–72.
   Google Scholar
• Gerwins, P., J. L. Blank, and G. L. Johnson 1997. Cloning of a novel mitogen-activated protein kinase kinase kinase, MEKK4, that selectively regulates the c-Jun amino terminal kinase pathway. J. Biol. Chem. 272: 8288–8295.
   PubMedGoogle Scholar
• Ginsberg, D., G. Vairo, T. Chittenden, Z. X. Xiao, G. Xu, K. L. Wydner, J. A. DeCaprio, J. B. Lawrence, and D. M. Livingston 1994. E2F-4, a new member of the E2F transcription factor family, interacts with p107. Genes Dev. 8: 2665–2679.
   PubMed Web of Science ®Google Scholar
• Glazer, R. I., and C. Rohlff 1994. Transcriptional regulation of multidrug resistance in breast cancer. Breast Cancer Res. Treat. 31: 263–271.
   PubMedGoogle Scholar
• Heidecker, G., M. Huleihel, J. L. Cleveland, W. Kolch, W. Beck, P. Lloyd, T. Pawson, and U. R. Rapp 1990. Mutational activation of c-Raf-1 and the definition of the minimal transforming sequence. Mol. Cell. Biol. 10: 2503–2512.
   PubMed Web of Science ®Google Scholar
• Hiebert, S. W., S. P. Chellappan, J. M. Horowitz, and J. R. Nevins 1992. The interaction of RB with E2F coincides with an inhibition of the transcriptional activity of E2F. Genes Dev. 6: 177–185.
   PubMed Web of Science ®Google Scholar
• Hinds, P. W., S. Mittnacht, V. Dulic, A. Arnold, S. I. Reed, and R. A. Weinberg 1992. Regulation of retinoblastoma protein functions by ectopic expression of human cyclins. Cell 70: 993–1006.
   PubMed Web of Science ®Google Scholar
• Hollingsworth, R. J., P. L. Chen, and W. H. Lee 1993. Integration of cell cycle control with transcriptional regulation by the retinoblastoma protein. Curr. Opin. Cell Biol. 5: 194–200.
   PubMed Web of Science ®Google Scholar
• Hollingsworth, R. J., C. E. Hensey, and W. H. Lee 1993. Retinoblastoma protein and the cell cycle. Curr. Opin. Genet. Dev. 3: 55–62.
   PubMedGoogle Scholar
• Horowitz, J. M. 1993. Regulation of transcription by the retinoblastoma protein. Genes Chromosomes Cancer 6: 124–131.
   PubMedGoogle Scholar
• Jelinek, T., P. Dent, T. W. Sturgill, and M. J. Weber 1996. Ras-induced activation of Raf-1 is dependent on tyrosine phosphorylation. Mol. Cell. Biol. 16: 1027–1034.
   PubMed Web of Science ®Google Scholar
• Jinno, S., K. Suto, A. Nagata, M. Igarashi, Y. Kanaoka, H. Nojima, and H. Okayama 1994. Cdc25A is a novel phosphatase functioning early in the cell cycle. EMBO J. 13: 1549–1556.
   PubMed Web of Science ®Google Scholar
• Johnson, D. G., J. K. Schwarz, W. D. Cress, and J. R. Nevins 1993. Expression of transcription factor E2F1 induces quiescent cells to enter S phase. Nature 365: 349–352.
   PubMed Web of Science ®Google Scholar
• Junaief, J. L., B. E. Strober, S. Guha, P. A. Khavari, K. Alin, J. Luban, M. Begenman, and S. P. Goff 1994. The retinoblastoma protein and Brg1 form a complex and co-operate to induce cell cycle arrest. Cell 79: 119–130.
   PubMedGoogle Scholar
• Kaelin, W. G.Jr., D. C. Pallas, J. A. DeCaprio, F. J. Kaye, and D. M. Livingston 1991. Identification of cellular proteins that can interact specifically with the T/E1A-binding region of the retinoblastoma gene product. Cell 64: 521–532.
   PubMed Web of Science ®Google Scholar
• Kato, J., H. Matsushime, S. W. Hiebert, M. E. Ewen, and C. J. Sherr 1993. Direct binding of cyclin D to the retinoblastoma gene product (pRb) and pRb phosphorylation by the cyclin D-dependent kinase CDK4. Genes Dev. 7: 331–342.
   PubMed Web of Science ®Google Scholar
• Kato, J. Y., M. Matsuoka, D. K. Strom, and C. J. Sherr 1994. Regulation of cyclin D-dependent kinase 4 (cdk4) by cdk4-activating kinase. Mol. Cell. Biol. 14: 2713–2721.
   PubMed Web of Science ®Google Scholar
• Kerkhoff, E., and U. R. Rapp 1997. Induction of cell proliferation in quiescent NIH 3T3 cells by oncogenic c-Raf-1. Mol. Cell. Biol. 17: 2576–2586.
   PubMed Web of Science ®Google Scholar
• La Thangue, N. 1994. DRTF1/E2F: an expanding family of heterodimeric transcription factors implicated in cell-cycle control. Trends Biochem. Sci. 19: 108–114.
   PubMed Web of Science ®Google Scholar
• Lee, C. S., A. deFazio, C. J. Ormandy, and R. L. Sutherland 1996. Inverse regulation of oestrogen receptor and epidermal growth factor receptor gene expression in MCF-7 breast cancer cells treated with phorbol ester. J. Steroid Biochem. Mol. Biol. 58: 267–275.
   PubMedGoogle Scholar
• Lee, E. Y., H. To, J. Y. Shew, R. Bookstein, P. Scully, and W. H. Lee 1988. Inactivation of the retinoblastoma susceptibility gene in human breast cancers. Science 241: 218–221.
   PubMed Web of Science ®Google Scholar
• Lee, W. H., Hollingsworth, R. E.Jr., Y. W. Qian, P. L. Chen, F. Hong, and E. Y. Lee 1991. RB protein as a cellular “corral” for growth-promoting proteins. Cold Spring Harbor Symp. Quant. Biol. 56: 211–217.
   PubMedGoogle Scholar
• Lees, J. A., K. J. Buchkovich, D. R. Marshak, C. W. Anderson, and E. Harlow 1991. The retinoblastoma protein is phosphorylated on multiple sites by human cdc2. EMBO J. 10: 4279–4290.
   PubMed Web of Science ®Google Scholar
• Lehman, T. A., M. Greenblatt, W. P. Bennett, and C. C. Harris 1994. Mutational spectrum of the p53 tumor suppressor gene: clues to cancer etiology and molecular pathogenesis. Drug Metab. Rev. 26: 221–235.
   PubMed Web of Science ®Google Scholar
• Lukas, J., J. Bartkova, and J. Bartek 1996. Convergence of mitogenic signaling cascades from diverse classes of receptors at the cyclin D-cyclin-dependent-kinase-pRb-controlled G1 checkpoint. Mol. Cell. Biol. 16: 6917–6925.
   PubMed Web of Science ®Google Scholar
• Lukas, J., J. Bartkova, M. Rohde, M. Strauss, and J. Bartek 1995. Cyclin D1 is dispensable for G1 control in retinoblastoma gene-deficient cells independently of cdk4 activity. Mol. Cell. Biol. 15: 2600–2611.
   PubMed Web of Science ®Google Scholar
• Lumpkin, C. J., T. L. Moore, M. D. Tarpley, J. M. Taylor, T. M. Badger, and J. K. McClung 1995. Acute ethanol and selected growth suppressor transcripts in regenerating rat liver. Alcohol 12: 357–362.
   PubMedGoogle Scholar
• Marais, R., Y. Light, H. F. Paterson, and C. J. Marshall 1995. Ras recruits Raf-1 to the membrane for activation by tyrosine phosphorylation. EMBO J. 14: 3136–3145.
   PubMed Web of Science ®Google Scholar
• Mark, H. F., G. Annas, R. Ricker, and J. Weitzel 1996. Clinical and research issues in breast cancer genetics. Ann. Clin. Lab. Sci. 26: 396–408.
   PubMedGoogle Scholar
• Mayol, S., J. Garriga, and X. Grana 1996. G1 cyclin/CDK-independent phosphorylation and accumulation of p130 during the transition from G1 to G0 lead to its association with E2F-4. Oncogene 13: 237–246.
   PubMedGoogle Scholar
• Mayol, S., X. Grana, A. Baldi, N. Sang, Q. Hu, and A. Giordano 1993. Cloning of a new member of the retinoblastoma gene family (pRb2) which binds to the E1A transforming domain. Oncogene 8: 2561–2566.
   PubMed Web of Science ®Google Scholar
• Mazzarelli, J. M., G. B. Atkins, J. V. Geisberg, and R. P. Ricciardi 1995. The viral oncoproteins Ad5 E1A, HPV16 E7 and SV40 TAg bind a common region of the TBP-associated factor-110. Oncogene 11: 1859–1864.
   PubMedGoogle Scholar
• McCarthy, S. A., M. L. Samuels, C. A. Pritchard, J. A. Abraham, and M. McMahon 1995. Rapid induction of heparin-binding epidermal growth factor/diphtheria toxin receptor expression by Raf and Ras oncogenes. Genes Dev. 9: 1953–1964.
   PubMed Web of Science ®Google Scholar
• McClung, J. K., D. B. Danner, D. A. Stewart, J. R. Smith, E. L. Schneider, C. K. Lumpkin, R. T. Dell’Orco, and M. J. Nuell 1989. Isolation of a cDNA hybrid that selects anti-proliferative mRNA from rat liver. Biochem. Biophys. Res. Commun. 164: 1316–1322.
   PubMedGoogle Scholar
• McClung, J. K., R. L. King, L. S. Walker, D. B. Danner, M. J. Nuell, C. A. Stewart, and R. T. Dell’Orco 1992. Expression of prohibitin, an antiproliferative protein. Exp. Gerontol. 27: 413–417.
   PubMedGoogle Scholar
• Meyerson, M., and E. Harlow 1994. Identification of G1 kinase activity for cdk6, a novel cyclin D partner. Mol. Cell. Biol. 14: 2077–2086.
   PubMed Web of Science ®Google Scholar
• Mischak, H., T. Seitz, P. Janosch, M. Eulitz, H. Steen, M. Schellerer, A. Philipp, and W. Koldh 1996. Negative regulation of Raf-1 by phosphorylation of serine 621. Mol. Cell. Biol. 16: 5409–5418.
   PubMedGoogle Scholar
• Morrison, D. K., D. R. Kaplan, J. A. Escobedo, U. R. Rapp, T. M. Roberts, and L. T. Williams 1989. Direct activation of the serine/threonine kinase activity of Raf-1 through tyrosine phosphorylation by the PDGF beta-receptor. Cell 58: 649–657.
   PubMed Web of Science ®Google Scholar
• Muller, R., D. Mumberg, and F. C. Lucibello 1993. Signals and genes in the control of cell cycle progression. Biochem. Biophys. Acta 1155: 151–179.
   PubMed Web of Science ®Google Scholar
• Murray, A. W. 1992. Creative blocks: cell cycle checkpoints and feedback controls. Nature 359: 599–604.
   PubMed Web of Science ®Google Scholar
• Murray, A. W., and T. Hunt 1993. The cell cycle: an introduction. Oxford University Press, Oxford, United Kingdom.
   Google Scholar
• Nevins, J. R. 1992. E2F: a link between the Rb tumor suppressor protein and viral oncoproteins. Science 258: 424–429.
   PubMed Web of Science ®Google Scholar
• Norbury, C., and P. Nurse 1992. Animal cell cycles and their control. Annu. Rev. Biochem. 61: 441–470.
   PubMed Web of Science ®Google Scholar
• Olah, Z., S. Komoly, N. Nagashima, F. Joo, U. R. Rappa, and W. B. Anderson 1991. Cerebral ischemia induces transient intracellular redistribution and intranuclear translocation of the Raf proto-oncogene product in hippocampal pyramidal cells. Exp. Brain Res. 84: 403–410.
   PubMedGoogle Scholar
• Peeper, D. S., T. M. Upton, M. H. Ladha, E. Neuman, J. Zalvide, R. Bernards, J. DeCaprio, and M. E. Ewen 1997. Ras signaling linked to the cell-cycle machinery by the retinoblastoma protein. Nature 386: 177–181.
   PubMed Web of Science ®Google Scholar
• Pritchard, C. A., M. L. Samuels, E. Bosch, and M. McMahon 1995. Conditionally oncogenic form of the A-Raf and B-Raf protein kinases display different biological and biochemical properties in NIH 3T3 cells. Mol. Cell. Biol. 15: 6430–6442.
   PubMed Web of Science ®Google Scholar
• Quelle, D. E., R. A. Ashmun, S. A. Shurtleff, J.-Y. Kato, D. Bar-Sagi, M. F. Roussel, and C. J. Sherr 1993. Overexpression of mouse D-type cyclins accelerates G1 phase in rodent fibroblasts. Genes Dev. 7: 1559–1571.
   PubMed Web of Science ®Google Scholar
• Rapp, U. R. 1991. Role of Raf-1 serine/threonine protein kinase in growth factor signal transduction. Oncogene 6: 495–500.
   PubMed Web of Science ®Google Scholar
• Resnitzky, D., M. Gossen, H. Bujard, and S. I. Reed 1994. Acceleration of G1/S transition by expression of cyclins D and E with an inducible system. Mol. Cell. Biol. 14: 1669–1679.
   PubMed Web of Science ®Google Scholar
• Samuels, M. L., and M. McMahon 1994. Inhibition of platelet-derived growth factor and epidermal growth factor-mediated mitogenesis and signaling in 3T3 cells expressing DRaf-1:ER, an estradiol-regulated form of Raf-1. Mol. Cell. Biol. 14: 7855–7866.
   PubMedGoogle Scholar
• Sardet, C., M. Vidal, D. Cobrinik, Y. Geng, C. Onufryk, A. Chen, and R. A. Weinberg 1995. E2F-4 and E2F-5, two members of the E2F family, are expressed in the early phases of the cell cycle. Proc. Natl. Acad. Sci. USA 92: 2403–2407.
   PubMedGoogle Scholar
• Serrano, M., G. J. Hannon, and D. Beach 1993. A new regulatory motif in cell-cycle control causing specific inhibition of cyclin D/CDK4. Nature 366: 704–707.
   PubMed Web of Science ®Google Scholar
• Sherr, C. J. 1994. The ins and outs of RB: coupling gene expression to the cell cycle clock. Trends Cell Biol. 4: 15–18.
   PubMedGoogle Scholar
• Shirodkar, S., M. Ewen, J. A. DeCaprio, J. Morgan, D. M. Livingston, and T. Chittenden 1992. The transcription factor E2F interacts with the retinoblastoma product and a p107-cyclin A complex in a cell cycle-regulated manner. Cell 68: 157–166.
   PubMed Web of Science ®Google Scholar
• Taya, Y. 1997. Rb kinases and RB-binding proteins: new points of view. Trends Biochem. Sci. 22: 14–17.
   PubMedGoogle Scholar
• Vojtek, A. B., S. M. Hollenberg, and J. A. Cooper 1993. Mammalian Ras interacts directly with the serine/threonine kinase Raf. Cell 74: 205–214.
   PubMed Web of Science ®Google Scholar
• Weinberg, R. A. 1995. The retinoblastoma protein and cell cycle control. Cell 81: 323–330.
   PubMed Web of Science ®Google Scholar
• Welch, P. J., and J. Y. J. Wang 1993. A C-terminal protein-binding domain in the retinoblastoma protein regulates nuclear c-Abl tyrosine kinase in the cell cycle. Cell 75: 779–790.
   PubMed Web of Science ®Google Scholar
• Welch, P. J., and J. Y. J. Wang 1995. Disruption of the retinoblastoma protein function by co-expression of its C pocket fragment. Genes Dev. 9: 31–46.
   PubMedGoogle Scholar
• Wong, K. K., X. Zou, K. T. Merrell, A. J. Patel, K. B. Marcu, S. Chellappan, and K. Calame 1995. v-Abl activates c-myc transcription through the E2F site. Mol. Cell. Biol. 15: 6535–6544.
   PubMedGoogle Scholar
• Woods, D., D. Parry, H. Cherwinski, E. Bosch, E. Lees, and M. McMahon 1997. Raf-induced proliferation or cell cycle arrest is determined by the level of Raf activity with arrest mediated by p21Cip1. Mol. Cell. Biol. 17: 5598–5611.
   PubMed Web of Science ®Google Scholar
• Yao, B., Y. Zhang, S. Delikat, S. Mathias, S. Basu, and R. Kolesnick 1995. Phosphorylation of Raf by ceramide-activated protein kinase. Nature 378: 307–310.
   PubMed Web of Science ®Google Scholar
• Zhu, L., S. van-den-Heuvel, K. Helin, A. Fattaey, M. Ewen, D. M. Livingston, N. Dyson, and E. Harlow 1993. Inhibition of cell proliferation by p107, a relative of the retinoblastoma protein. Genes Dev. 7: 1111–1125.
   PubMed Web of Science ®Google Scholar
• Zou, X., S. Rudchenko, K.-K. Wong, and K. Calame 1997. Induction of c-myc transcription by the v-Abl tyrosine kinase requires Ras, Raf-1 and cyclin-dependent kinases. Genes Dev. 11: 654–662.
   PubMedGoogle Scholar