Atypical Protein Kinase Cs Are the Ras Effectors That Mediate Repression of Myogenic Satellite Cell Differentiation

REFERENCES

• Bandyopadhyay, G., M. L. Standaert, U. Kikkawa, Y. Ono, J. Moscat, and R. V. Farese. 1999. Effects of transiently expressed atypical (zeta, lambda), conventional (alpha, beta) and novel (delta, epsilon) protein kinase C isoforms on insulin-stimulated translocation of epitope-tagged GLUT4 glucose transporters in rat adipocytes: specific interchangeable effects of protein kinases C-zeta and C-lambda. Biochem. J. 337: 461–470.
   PubMedGoogle Scholar
• Berra, E., M. T. Diaz-Meco, I. Dominguez, M. M. Municio, L. Sanz, J. Lozano, R. S. Chapkin, and J. Moscat. 1993. Protein kinase C zeta isoform is critical for mitogenic signal transduction. Cell 74: 555–563.
   PubMed Web of Science ®Google Scholar
• Campbell, S. L., R. Khosravi-Far, K. L. Rossman, G. J. Clark, and C. J. Der. 1998. Increasing complexity of Ras signaling. Oncogene 17: 1395–1413.
   PubMed Web of Science ®Google Scholar
• Clegg, C. H., T. A. Linkhart, B. B. Olwin, and S. D. Hauschka. 1987. Growth factor control of skeletal muscle differentiation: commitment to terminal differentiation occurs in G1 phase and is repressed by fibroblast growth factor. J. Cell Biol. 105: 949–956.
   PubMed Web of Science ®Google Scholar
• Cooper, D. R., J. E. Watson, M. Acevedo-Duncan, R. J. Pollet, M. L. Standaert, and R. V. Farese. 1989. Retention of specific protein kinase C isozymes following chronic phorbol ester treatment in BC3H-1 myocytes. Biochem. Biophys. Res. Commun. 161: 327–334.
   PubMedGoogle Scholar
• Crespo, P., H. Mischak, and J. S. Gutkind. 1995. Overexpression of mammalian protein kinase C-zeta does not affect the growth characteristics of NIH 3T3 cells Biochem. Biophys. Res. Commun. 213: 266–272.
   PubMedGoogle Scholar
• Diaz-Meco, M. T., J. Lozano, M. M. Municio, E. Berra, S. Frutos, L. Sanz, and J. Moscat. 1994. Evidence for the in vitro and in vivo interaction of Ras with protein kinase C zeta. J. Biol. Chem. 269: 31706–31710.
   PubMedGoogle Scholar
• Dominguez, I., M. T. Diaz-Meco, M. M. Municio, E. Berra, A. Garcia de Herreros, M. E. Cornet, L. Sanz, and J. Moscat. 1992. Evidence for a role of protein kinase C zeta subspecies in maturation of Xenopus laevis oocytes. Mol. Cell. Biol. 12: 3776–3783.
   PubMed Web of Science ®Google Scholar
• Fedorov, Y. V., N. C. Jones, and B. B. Olwin. 1998. Regulation of myogenesis by fibroblast growth factors requires beta- gamma subunits of pertussis toxin-sensitive G proteins. Mol. Cell. Biol. 18: 5780–5787.
   PubMedGoogle Scholar
• Fedorov, Y. V., R. S. Rosenthal, and B. B. Olwin. 2001. Oncogenic ras-induced proliferation requires autocrine fibroblast growth factor 2 signaling in skeletal muscle cells. J. Cell Biol. 152: 1301–1306.
   PubMedGoogle Scholar
• Flanagan-Steet, H., K. Hannon, M. J. McAvoy, R. Hullinger, and B. B. Olwin. 2000. Loss of FGF receptor 1 signaling reduces skeletal muscle mass and disrupts myofiber organization in the developing limb. Dev. Biol. 218: 21–37.
   PubMedGoogle Scholar
• Garcia-Paramio, P., Y. Cabrerizo, F. Bornancin, P. J. Parker, D. Toullec, P. Pianetti, H. Coste, P. Bellevergue, T. Grand-Perret, M. Ajakane, V. Baudet, P. Boissin, E. Boursier, F. Loriolle, et al. 1998. The broad specificity of dominant inhibitory protein kinase C mutants infers a common step in phosphorylation. Biochem. J. 333: 631–636.
   PubMed Web of Science ®Google Scholar
• Gschwendt, M., S. Dieterich, J. Rennecke, W. Kittstein, H. J. Mueller, F. J. Johannes, G. Bandyopadhyay, M. L. Standaert, U. Kikkawa, Y. Ono, J. Moscat, and R. V. Farese. 1996. Inhibition of protein kinase C mu by various inhibitors. Differentiation from protein kinase c isoenzymes. FEBS Lett. 392: 77–80.
   PubMed Web of Science ®Google Scholar
• Jones, N. C., Y. V. Fedorov, R. S. Rosenthal, and B. B. Olwin. 2001. ERK1/2 is required for myoblast proliferation but is dispensable for muscle gene expression and cell fusion. J. Cell. Physiol. 186: 104–115.
   PubMedGoogle Scholar
• Kampfer, S., K. Hellbert, A. Villunger, W. Doppler, G. Baier, H. H. Grunicke, F. Uberall, G. Bandyopadhyay, M. L. Standaert, U. Kikkawa, Y. Ono, J. Moscat, and R. V. Farese. 1998. Transcriptional activation of c-fos by oncogenic Ha-Ras in mouse mammary epithelial cells requires the combined activities of PKC-lambda, epsilon and zeta. EMBO J. 17: 4046–4055.
   PubMedGoogle Scholar
• Khosravi-Far, R., M. A. White, J. K. Westwick, P. A. Solski, M. Chrzanowska-Wodnicka, L. Van Aelst, M. H. Wigler, and C. J. Der. 1996. Oncogenic Ras activation of Raf/mitogen-activated protein kinase-independent pathways is sufficient to cause tumorigenic transformation. Mol. Cell. Biol. 16: 3923–3933.
   PubMed Web of Science ®Google Scholar
• Konieczny, S. F., B. L. Drobes, S. L. Menke, and E. J. Taparowsky. 1989. Inhibition of myogenic differentiation by the H-ras oncogene is associated with the down regulation of the MyoD1 gene. Oncogene 4: 473–481.
   PubMedGoogle Scholar
• Kudla, A. J., M. L. John, D. F. Bowen-Pope, B. Rainish, and B. B. Olwin. 1995. A requirement for fibroblast growth factor in regulation of skeletal muscle growth and differentiation cannot be replaced by activation of platelet-derived growth factor signaling pathways. Mol. Cell. Biol. 15: 3238–3246.
   PubMedGoogle Scholar
• Kudla, A. J., N. C. Jones, R. S. Rosenthal, K. Arthur, K. L. Clase, and B. B. Olwin. 1998. The FGF receptor-1 tyrosine kinase domain regulates myogenesis but is not sufficient to stimulate proliferation. J. Cell Biol. 142: 241–250.
   PubMedGoogle Scholar
• Lim, Y. P., B. C. Low, J. Lim, E. S. Wong, and G. R. Guy. 1999. Association of atypical protein kinase C isotypes with the docker protein FRS2 in fibroblast growth factor signaling. J. Biol. Chem. 274: 19025–19034.
   PubMedGoogle Scholar
• Linkhart, T. A., C. H. Clegg, and S. D. Hauschka. 1980. Control of mouse myoblast commitment to terminal differentiation by mitogens. J. Supramol. Struct. 14: 483–498.
   PubMedGoogle Scholar
• Mitin, N., A. J. Kudla, S. F. Konieczny, and E. J. Taparowsky. 2001. Differential effects of Ras signaling through NFkappaB on skeletal myogenesis. Oncogene 20: 1276–1286.
   PubMedGoogle Scholar
• Nishizuka, Y., F. Uberall, K. Hellbert, S. Kampfer, K. Maly, A. Villunger, M. Spitaler, J. Mwanjewe, G. Baier-Bitterlich, G. Baier, and H. H. Grunicke. 1992. Intracellular signaling by hydrolysis of phospholipids and activation of protein kinase C. Science 258: 607–614.
   PubMed Web of Science ®Google Scholar
• Nishizuka, Y., F. Uberall, K. Hellbert, S. Kampfer, K. Maly, A. Villunger, M. Spitaler, J. Mwanjewe, G. Baier-Bitterlich, G. Baier, and H. H. Grunicke. 1995. Protein kinase C and lipid signaling for sustained cellular responses. FASEB J. 9: 484–496.
   PubMed Web of Science ®Google Scholar
• Olson, E. N., G. Spizz, and M. A. Tainsky. 1987. The oncogenic forms of N-ras or H-ras prevent skeletal myoblast differentiation. Mol. Cell. Biol. 7: 2104–2111.
   PubMed Web of Science ®Google Scholar
• Ramocki, M. B., S. E. Johnson, M. A. White, C. L. Ashendel, S. F. Konieczny, and E. J. Taparowsky. 1997. Signaling through mitogen-activated protein kinase and Rac/Rho does not duplicate the effects of activated Ras on skeletal myogenesis. Mol. Cell. Biol. 17: 3547–3555.
   PubMed Web of Science ®Google Scholar
• Ramocki, M. B., M. A. White, S. F. Konieczny, and E. J. Taparowsky. 1998. A role for RalGDS and a novel Ras effector in the Ras-mediated inhibition of skeletal myogenesis. J. Biol. Chem. 273: 17696–17701.
   PubMedGoogle Scholar
• Rando, T. A., and H. M. Blau. 1994. Primary mouse myoblast purification, characterization, and transplantation for cell-mediated gene therapy J. Cell Biol. 125: 1275–1287.
   Google Scholar
• Sanes, J. R., J. L. Rubenstein, J. F. Nicolas, G. Bandyopadhyay, M. L. Standaert, U. Kikkawa, Y. Ono, J. Moscat, and R. V. Farese. 1986. Use of a recombinant retrovirus to study post-implantation cell lineage in mouse embryos. EMBO J. 5: 3133–3142.
   PubMed Web of Science ®Google Scholar
• Stratton, M. R., C. Fisher, B. A. Gusterson, and C. S. Cooper. 1989. Detection of point mutations in N-ras and K-ras genes of human embryonal rhabdomyosarcomas using oligonucleotide probes and the polymerase chain reaction. Cancer Res. 49: 6324–6327.
   PubMed Web of Science ®Google Scholar
• Toker, A., F. Uberall, K. Hellbert, S. Kampfer, K. Maly, A. Villunger, M. Spitaler, J. Mwanjewe, G. Baier-Bitterlich, G. Baier, and H. H. Grunicke. 1998. Signaling through protein kinase C. Front. Biosci. 3: D1134–D1147.
   PubMedGoogle Scholar
• Toullec, D., P. Pianetti, H. Coste, P. Bellevergue, T. Grand-Perret, M. Ajakane, V. Baudet, P. Boissin, E. Boursier, F. Loriolle, et al. 1991. The bisindolylmaleimide GF 109203X is a potent and selective inhibitor of protein kinase C. J. Biol. Chem. 266: 15771–15781.
   PubMed Web of Science ®Google Scholar
• Uberall, F., K. Hellbert, S. Kampfer, K. Maly, A. Villunger, M. Spitaler, J. Mwanjewe, G. Baier-Bitterlich, G. Baier, and H. H. Grunicke. 1999. Evidence that atypical protein kinase C-lambda and atypical protein kinase C-zeta participate in Ras-mediated reorganization of the F-actin cytoskeleton. J. Cell Biol. 144: 413–425.
   PubMedGoogle Scholar
• White, M. A., C. Nicolette, A. Minden, A. Polverino, L. Van Aelst, M. Karin, and M. H. Wigler. 1995. Multiple Ras functions can contribute to mammalian cell transformation. Cell 80: 533–541.
   PubMed Web of Science ®Google Scholar
• Xu, S., and M. H. Cobb. 1997. MEKK1 binds directly to the c-Jun N-terminal kinases/stress-activated protein kinases. J. Biol. Chem. 272: 32056–32060.
   PubMed Web of Science ®Google Scholar