Abstract
The interaction between growth factors and their cell surface receptors initiates the cell cycle which under different physiological conditions can lead to cell growth, differentiation, survival or apoptosis (programmed cell death) (Figure 1). The sequence of events leading to cellular proliferation induced by growth factors involves activation of an intracellular signaling cascade resulting in induction of the expression of specific target genes in the nucleus which are sequentially and temporally expressed in defined classes, such as immediate early, delayed early and late. These gene products encode a large number of proteins which collaborate and indeed some are essential for driving cells through Gap1 (G1) of the cell cycle and into DNA synthesis (S phase). For successful entry into S phase, the growth factor must be in continuous contact with the cells. If however, the growth factor is removed prior to late G1 (R), cells will not commit to S phase and instead arrest in G1. This commitment step is controlled at least in part by certain members of a family of gene products, the cyclins, which are differentially regulated during the course of the cell cycle (Figure 1).
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References
Askew, D.S., R.A. Ashmun, B.C. Simmons and J.L. Cleveland. 1991. Constitutive c-myc expression in an IL-3 dependent myeloid cell line suppresses cell cycle arrest an accelerates apoptosis. Oncogene 6: 1915–1922.
Askew, D.S., J.N. Ihle and J.L. Cleveland. Activation of apoptosis associated with enforced Myc expression in myeloid progenitor cells in dominant to the suppression of apoptosis by interleukin-3 or Erythropoietin. Blood (in press).
Bruder, J.T., G. Heidecker, and U. R. Rapp UR. 1992. Serum-, TP A- and Ras-induced expression from Ap-1/Ets-driven promoters requires Raf-1 kinase. Genes & Dev 6: 545–556.
Buscher, D., P. Dello Sbarba, R.A. Hipskind, U.R. Rapp, E.R. Stanley and M. Baccarini. 1993. v-raf confers CSF-1 independent growth to a macrophage cell line and leads to immediate early gene expression without MAP-kinase activation. Oncogene 8: 3323–3332.
Cai, H., P. Erhardt, J. Troppmair, M.T. Diaz-Meco, G. Sithanandam, U.R. Rapp, J. Moscat, G.M. Cooper. 1993. Hydrolysis of phosphatidylcholine couples Ras to activation of Raf protein kinase during mitogenic signal transduction. Mol. Cell. Biol. 13: 7645–7651.
Cleveland, J., M. Jansen, K. Bister, T. Fredrickson, H. Morse, J. Ihle, and U. Rapp. 1986. Interaction between raf and myc oncogenes in transformation in vivo and in vitro. J. Cell Biochem. 30: 185–218.
Cleveland, J.L., M. Dean, N. Rosenberg, J. Y-J. Wang and U.R. Rapp. 1989. Tyrosine kinase oncogenes abrogate interieukin-3 dependence of murine myeloid cells through signalling pathways involving c-myc: Conditional regulation of c-myc transcription by temperature sensitive v-abl. Mol. Cell. Biol. 9: 5685–5695.
Cleveland, J.L., J. Troppmair, D.S. Askew, P. Lloyd, J.N. Ihle and U.R. Rapp. 1994. Raf-1 is required for optimal growth of interleukin-3- dependent myeloid cells and synergizes with Myc to promote autonomous growth by suppressing apoptosis.
Crespo, P., N. Xuf J. Daniotti, J. Troppmair, U.R. Rapp, and J.S. Gutkind. Signalling through transforming G protein-coupled receptors in NIH3T3 cells involves c-Raf activation: evidence for a protein kinase C independent pathway. (Submitted).
Finco, T.S. and A.S. Baldwin. 1993. KB site dependent induction of gene expression by diverse inducers of nuclear factor KB requires Raf-1. J. Biol. Chem. 268: 17676–17679.
Gu, W., K. Bhatia, I.T. Magrath, C.V. Dang, and R. Dalla-Favera. 1994. Binding and suppression of the Myc transcriptional activation domain by p107. Science 264: 251–254.
Heikkila, R., G. Schwab, E. Wickstrom, S.L. Lohie, D. H. Pliznik, R. Watt, and L. M. Nacres. 1987. A c-myc antisense oligonucleotide inhibits entry into S-phase but not progression from Go to G1. Nature (London) 328: 445–449.
Herschback, B.M. and A.D. Johnson. 1993. Transcriptional repression in eukaryotes. Annu. Rev. Cell Biol. 9: 479–509.
Koff, A., M. Ohtsuki, K., Polyak, J. Roberts, and J. Massague. 1993. Negative regulation of G1 in mammalian cells: inhibition of cyclin- dependent kinase by TGF-beta. Science 260: 536–539.
Kolesnick, R. and D.W. Golde. 1994. The sphingomyelin pathway in tumor necrosis factor and interleukin-1 signaling. Cell, 77: 325–328.
Kolch, W., G. Heidecker, and U. R. Rapp. 1991. Raf-1 protein kinase is required for growth of induced NIH/3T3 cells. Nature 349: 426–428.
Kyriakis, J.M., P. Banerjee, E. Nikolakaki, T. Dal, E.A. Rube, M.F. Ahmad, J. Avruch and J.R. Woodgett. 1994. The stress-activated protein kinase subfamily of c-Jun kinases. Nature 369: 156–160.
La Rosa, F.A., J.W. Pierce and G.E. Sonenshein. 1994. Differential regulation of the c-myc oncogene promoter by the NF-kB/rel family of transcription factors. Mol. Cell. Biol. 14: 1039–1044.
Leevers, S.J., H.G. Paterson and C. J. Marshall. 1994. Requirement for Ras in Raf activation is overcome by targeting Raf. Nature 369: 411–414.
Loh, C., C. Romeo, B. Seed, J.T. Bruder, U. Rapp and A. Rao. 1994. Association of Raf with the CD3 delta and gamma chains of the T cell receptor-CD3 complex. J. Biol. Chem. 269: 8817–8825.
Magnuson, N.S., T. Beck, H. Vahidi, H. Hahn, U. Smola and U.R. Rapp. The raf-1 serine/threoine protein kinase. In: Herrmann, R. and R. Mertelsmann (eds): Hematopoietic growth factors in clinical applications. 2nd ed. (in press).
Marcu.K. B., S.A. Bossone, and A.J. Patel. 1992. Myc function and regulation. Ann. Rev. Biochem. 61: 809–860.
Maslinski, W., B. Remillard, M. Tsudo and T.B. Strom. 1992. lnterleukin-2 (IL-2) induces tyrosine kinase-dependent translocation of active raf-1 from the IL-2 receptor into the cytosol. J. Biol. Chem. 267: 15281–15284.
Miyashita, T., L. Hovey, T. Torigoe, S. Krajewsky, J. Troppmair, U.R. Rapp and J.C. Reed. Novel form of oncogene cooperation: synergistic suppression of apoptosis by combination of bcl-2 and raf oncogenes. Oncogene (in press).
Moodie SA, B.M. Willumsen, M.J. Webber, and A. Wolfman. 1993. Complexes of Ras-GTP with Raf-1 and mitogen-activated protein kinase kinase. Science 260: 1658–1661.
Munger, K., J. Pietenpol, M. Pittelkow, J. Holt, and H. Moses. 1992. Transforming growth factor beta-1 regulation of c-myc expression, pRB phosphorylation, and cell cycle progression in keratinocytes. Cell Growth Differ. 3: 291–298.
Porras, A., K. Muszynski, U.R. Rapp and E. Santos. 1994. Dissociation between activation of Raf-1 kinase and the 42-kDa mitogen-activated protein kinase/90-kDa S6 kinase (MAPK/RSK) cascade in the insulin/Ras pathway of adipocytic differentiaion of 3T3 L1 cells. J. Biol. Chem. 269: 12741–12748.
Rapp U.R., J. T. Bruder, and J. Troppmair. 1993. Role of the Raf signal transduction pathway in fos/jun regulation and determination of cell fates. CRC, Crit. Rev. (in press).
Reed, J.C., S. Yum, M.P. Cuddy, B.C. Turner, and U.R. Rapp. 1991. Differential regulation of the p72-74 Raf-1 kinase in 3T3 fibroblasts expressing ras or src oncogenes. Cell Growth Diff. 2: 235–243.
Sato, T., M. Hanada, S. Bodrug, S. Irie, N. Iwama, L. Boise, C. Thompson, E. Golemis, L. Fong, H-G. Wang and J.C. Reed. Investigations of interactions between members of the Bcl-2 protein family using yeast two-hybrid system, (submitted).
Stokoe, D., S.G. Macdonald, K. Cadwallader, M. Symons, and J. Hancock. 1994. Activation of Raf as a result of recruitment to the plasma membrane. Science, 264: 1463–1467.
Thomas, S.M., M. De Marco, G. D’Arcangelo, S. Halegoua, J.S. Brugge. 1992. Ras is essential for nerve growth factor- and phorbol ester- induced tyrosine phosphorylation of MAP kinases. Cell 68: 1031–1046.
Troppmair, J., J.T. Bruder, H. App, H. Cai, L. Liptak, J. Szeberenyi, G.M. Cooper and U.R. Rapp. 1992. Ras controls coupling of growth factor receptors and protein kinase C in the membrane to Raf-1 and B-Raf protein serine kinases in the cytosol. Oncogene 7: 1867–1873.
Troppmair, J., J. T. Bruder, H. Munoz, P.A. Lloyd, J. Kyriakis, P. Banerjee, J. Avruch and U.R. Rapp. 1994. Mitogen-activated protein kinase/extracellular signal-regulated protein kinase activation by oncogenes, serum and 12-O-tetradecanoylphorbol-13-acetate requires raf and is necessary for transformation. J. Biol. Chem. 269: 7030–7035.
Troppmair, J., M. Huleihel, J. Cleveland, J.F. Mushinski, J. Kurie, H.C. Morse, III, J.S. Was, M. Potter and U.R. Rapp. 1988. Plasmacytoma induction by J series of v-myc recombinant retroviruses: Evidence for the requirement of two (raf and myc) oncogenes for transformation. Current Topics in Micro. Immun. 141: 110–114.
Van Aelst L, M. Barr, S. Marcus, A. Polverino, and M. Wigler. 1993. Complex formation between RAS and RAF and other protein kinases. Proc Natl Acad Sci USA 90: 6213–6217.
Vaux, D., S. Cory, and J. Adams. 1988. Bcl-2 gene promotes hematopoietic cell survival and cooperates with c-myc to immortalize pre-B cells. Nature 335: 440–442.
Vojtek AB, S.M. Hollenberg, J.A. Cooper. 1993. Mammalian Ras interacts directly with the serine/threonine kinase Raf. Cell 74: 205–214.
Warner PH, P.R. Viciana, and J. Downward. 1993. Direct interaction of Ras and the amino-terminal region of Raf-1 in vitro. Nature (Lond) 364: 352–355.
Zhang X-f, J. Settleman, J.M. Kyriakis, E. Takeuchi-Suzuki, Elledge, M.S. Marshall, J.T. Bruder, U.R. Rapp,and J. Avruch. 1993. Normal and oncogenic p21ras proteins bind to the amino-terminal regulatory domain of c-Raf-1. Nature. 364: 308–313.
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Beck, T.W., Magnuson, N.S., Rapp, U.R. (1995). Growth Factor Regulation of Cell Cycle Progression and Cell Fate Determination. In: Potter, M., Melchers, F. (eds) Mechanisms in B-Cell Neoplasia 1994. Current Topics in Microbiology and Immunology, vol 194. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-79275-5_34
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DOI: https://doi.org/10.1007/978-3-642-79275-5_34
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