Myocyte Enhancer Factor 2 Acetylation by p300 Enhances Its DNA Binding Activity, Transcriptional Activity, and Myogenic Differentiation

REFERENCES

• Black, B. L., and E. N. Olson. 1998. Transcriptional control of muscle development by myocyte enhancer factor-2 (MEF2) proteins. Annu. Rev. Cell Dev. Biol. 14:167–196.
   PubMed Web of Science ®Google Scholar
• Breitbart, R. E., C. S. Liang, L. B. Smoot, D. A. Laheru, V. Mahdavi, and B. Nadal-Ginard. 1993. A fourth human MEF2 transcription factor, hMEF2D, is an early marker of the myogenic lineage. Development 118:1095–1106.
   PubMed Web of Science ®Google Scholar
• Breitschopf, K., E. Bengal, T. Ziv, A. Admon, and A. Ciechanover. 1998. A novel site for ubiquitination: the N-terminal residue, and not internal lysines of MyoD, is essential for conjugation and degradation of the protein. EMBO J. 17:5964–5973.
   PubMed Web of Science ®Google Scholar
• Brooks, C. L., and W. Gu. 2003. Ubiquitination, phosphorylation and acetylation: the molecular basis for p53 regulation. Curr. Opin. Cell Biol. 15:164–171.
   PubMed Web of Science ®Google Scholar
• Buchberger, A., K. Ragge, and H. H. Arnold. 1994. The myogenin gene is activated during myocyte differentiation by pre-existing, not newly synthesized transcription factor MEF-2. J. Biol. Chem. 269:17289–17296.
   PubMed Web of Science ®Google Scholar
• Chan, J. K., L. Sun, X. J. Yang, G. Zhu, and Z. Wu. 2003. Functional characterization of an amino-terminal region of HDAC4 that possesses MEF2 binding and transcriptional repressive activity. J. Biol. Chem. 278:23515–23521.
   PubMedGoogle Scholar
• Cheng, T. C., M. C. Wallace, J. P. Merlie, and E. N. Olson. 1993. Separable regulatory elements governing myogenin transcription in mouse embryogenesis. Science 261:215–218.
   PubMed Web of Science ®Google Scholar
• Eckner, R., M. E. Ewen, D. Newsome, M. Gerdes, J. A. DeCaprio, J. B. Lawrence, and D. M. Livingston. 1994. Molecular cloning and functional analysis of the adenovirus E1A-associated 300-kD protein (p300) reveals a protein with properties of a transcriptional adaptor. Genes Dev. 8:869–884.
   PubMed Web of Science ®Google Scholar
• Fulco, M., R. L. Schiltz, S. Iezzi, M. T. King, P. Zhao, Y. Kashiwaya, E. Hoffman, R. L. Veech, and V. Sartorelli. 2003. Sir2 regulates skeletal muscle differentiation as a potential sensor of the redox state. Mol. Cell 12:51–62.
   PubMed Web of Science ®Google Scholar
• Gu, W., and R. G. Roeder. 1997. Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain. Cell 90:595–606.
   PubMed Web of Science ®Google Scholar
• Han, J., Y. Jiang, Z. Li, V. V. Kravchenko, and R. J. Ulevitch. 1997. Activation of the transcription factor MEF2C by the MAP kinase p38 in inflammation. Nature 386:296–299.
   PubMed Web of Science ®Google Scholar
• Hayashi, M., S. W. Kim, K. Imanaka-Yoshida, T. Yoshida, E. D. Abel, B. Eliceiri, Y. Yang, R. J. Ulevitch, and J. D. Lee. 2004. Targeted deletion of BMK1/ERK5 in adult mice perturbs vascular integrity and leads to endothelial failure. J. Clin. Investig. 113:1138–1148.
   PubMedGoogle Scholar
• Kato, Y., V. V. Kravchenko, R. I. Tapping, J. Han, R. J. Ulevitch, and J. D. Lee. 1997. BMK1/ERK5 regulates serum-induced early gene expression through transcription factor MEF2C. EMBO J. 16:7054–7066.
   PubMed Web of Science ®Google Scholar
• Kuo, M. H., and C. D. Allis. 1998. Roles of histone acetyltransferases and deacetylases in gene regulation. Bioessays 20:615–626.
   PubMed Web of Science ®Google Scholar
• Li, L., J. Zhou, G. James, R. Heller-Harrison, M. P. Czech, and E. N. Olson. 1992. FGF inactivates myogenic helix-loop-helix proteins through phosphorylation of a conserved protein kinase C site in their DNA-binding domains. Cell 71:1181–1194.
   PubMed Web of Science ®Google Scholar
• Lilly, B., B. Zhao, G. Ranganayakulu, B. M. Paterson, R. A. Schulz, and E. N. Olson. 1995. Requirement of MADS domain transcription factor D-MEF2 for muscle formation in Drosophila. Science 267:688–693.
   PubMed Web of Science ®Google Scholar
• Lin, Q., J. Schwarz, C. Bucana, and E. N. Olson. 1997. Control of mouse cardiac morphogenesis and myogenesis by transcription factor MEF2C. Science 276:1404–1407.
   PubMed Web of Science ®Google Scholar
• Mal, A., M. Sturniolo, R. L. Schiltz, M. K. Ghosh, and M. L. Harter. 2001. A role for histone deacetylase HDAC1 in modulating the transcriptional activity of MyoD: inhibition of the myogenic program. EMBO J. 20:1739–1753.
   PubMed Web of Science ®Google Scholar
• Mao, Z., A. Bonni, F. Xia, M. Nadal-Vicens, and M. E. Greenberg. 1999. Neuronal activity-dependent cell survival mediated by transcription factor MEF2. Science 286:785–790.
   PubMed Web of Science ®Google Scholar
• McKinsey, T. A., C. L. Zhang, and E. N. Olson. 2001. Control of muscle development by dueling HATs and HDACs. Curr. Opin. Genet. Dev. 11:497–504.
   PubMed Web of Science ®Google Scholar
• McKinsey, T. A., C. L. Zhang, and E. N. Olson. 2002. Signaling chromatin to make muscle. Curr. Opin. Cell Biol. 14:763–772.
   PubMed Web of Science ®Google Scholar
• Molinari, S., F. Relaix, M. Lemonnier, B. Kirschbaum, B. Schafer, and M. Buckingham. 2004. A novel complex regulates cardiac actin gene expression through interaction of Emb, a class VI POU domain protein, MEF2D, and the histone transacetylase p300. Mol. Cell. Biol. 24:2944–2957.
   PubMedGoogle Scholar
• Molkentin, J. D., B. L. Black, J. F. Martin, and E. N. Olson. 1995. Cooperative activation of muscle gene expression by MEF2 and myogenic bHLH proteins. Cell 83:1125–1136.
   PubMedGoogle Scholar
• Molkentin, J. D., and E. N. Olson. 1996. Defining the regulatory networks for muscle development. Curr. Opin. Genet. Dev. 6:445–453.
   PubMed Web of Science ®Google Scholar
• Mymryk, J. S., R. W. Lee, and S. T. Bayley. 1992. Ability of adenovirus 5 E1A proteins to suppress differentiation of BC3H1 myoblasts correlates with their binding to a 300 kDa cellular protein. Mol. Biol. Cell 3:1107–1115.
   PubMedGoogle Scholar
• Naya, F. J., B. L. Black, H. Wu, R. Bassel-Duby, J. A. Richardson, J. A. Hill, and E. N. Olson. 2002. Mitochondrial deficiency and cardiac sudden death in mice lacking the MEF2A transcription factor. Nat. Med. 8:1303–1309.
   PubMedGoogle Scholar
• Polesskaya, A., and A. Harel-Bellan. 2001. Acetylation of MyoD by p300 requires more than its histone acetyltransferase domain. J. Biol. Chem. 276:44502–44503.
   PubMedGoogle Scholar
• Puri, P. L., M. L. Avantaggiati, C. Balsano, N. Sang, A. Graessmann, A. Giordano, and M. Levrero. 1997. p300 is required for MyoD-dependent cell cycle arrest and muscle-specific gene transcription. EMBO J. 16:369–383.
   PubMed Web of Science ®Google Scholar
• Puri, P. L., V. Sartorelli, X. J. Yang, Y. Hamamori, V. V. Ogryzko, B. H. Howard, L. Kedes, J. Y. Wang, A. Graessmann, Y. Nakatani, and M. Levrero. 1997. Differential roles of p300 and PCAF acetyltransferases in muscle differentiation. Mol. Cell 1:35–45.
   PubMed Web of Science ®Google Scholar
• Roth, J. F., N. Shikama, C. Henzen, I. Desbaillets, W. Lutz, S. Marino, J. Wittwer, H. Schorle, M. Gassmann, and R. Eckner. 2003. Differential role of p300 and CBP acetyltransferase during myogenesis: p300 acts upstream of MyoD and Myf5. EMBO J. 22:5186–5196.
   PubMed Web of Science ®Google Scholar
• Sartorelli, V., J. Huang, Y. Hamamori, and L. Kedes. 1997. Molecular mechanisms of myogenic coactivation by p300: direct interaction with the activation domain of MyoD and with the MADS box of MEF2C. Mol. Cell. Biol. 17:1010–1026.
   PubMed Web of Science ®Google Scholar
• Sartorelli, V., P. L. Puri, Y. Hamamori, V. Ogryzko, G. Chung, Y. Nakatani, J. Y. Wang, and L. Kedes. 1999. Acetylation of MyoD directed by PCAF is necessary for the execution of the muscle program. Mol. Cell 4:725–734.
   PubMed Web of Science ®Google Scholar
• Song, A., Q. Wang, M. G. Goebl, and M. A. Harrington. 1998. Phosphorylation of nuclear MyoD is required for its rapid degradation. Mol. Cell. Biol. 18:4994–4999.
   PubMed Web of Science ®Google Scholar
• Spicer, D. B., J. Rhee, W. L. Cheung, and A. B. Lassar. 1996. Inhibition of myogenic bHLH and MEF2 transcription factors by the bHLH protein Twist. Science 272:1476–1480.
   PubMed Web of Science ®Google Scholar
• Sun, L., L. Liu, X. J. Yang, and Z. Wu. 2004. Akt binds prohibitin 2 and relieves its repression of MyoD and muscle differentiation. J. Cell Sci. 117:3021–3029.
   PubMedGoogle Scholar
• Wang, L., C. Fan, S. E. Topol, E. J. Topol, and Q. Wang. 2003. Mutation of MEF2A in an inherited disorder with features of coronary artery disease. Science 302:1578–1581.
   PubMed Web of Science ®Google Scholar
• Wu, Z., P. J. Woodring, K. S. Bhakta, K. Tamura, F. Wen, J. R. Feramisco, M. Karin, J. Y. Wang, and P. L. Puri. 2000. p38 and extracellular signal-regulated kinases regulate the myogenic program at multiple steps. Mol. Cell. Biol. 20:3951–3964.
   PubMed Web of Science ®Google Scholar
• Xu, Q., and Z. Wu. 2000. The insulin-like growth factor-phosphatidylinositol 3-kinase-Akt signaling pathway regulates myogenin expression in normal myogenic cells but not in rhabdomyosarcoma-derived RD cells. J. Biol. Chem. 275:36750–36757.
   PubMed Web of Science ®Google Scholar
• Yee, S. P., and P. W. Rigby. 1993. The regulation of myogenin gene expression during the embryonic development of the mouse. Genes Dev. 7:1277–1289.
   PubMed Web of Science ®Google Scholar
• Youn, H. D., L. Sun, R. Prywes, and J. O. Liu. 1999. Apoptosis of T cells mediated by Ca2+-induced release of the transcription factor MEF2. Science 286:790–793.
   PubMed Web of Science ®Google Scholar
• Yun, K., and B. Wold. 1996. Skeletal muscle determination and differentiation: story of a core regulatory network and its context. Curr. Opin. Cell Biol. 8:877–889.
   PubMed Web of Science ®Google Scholar
• Zhao, M., L. New, V. V. Kravchenko, Y. Kato, H. Gram, F. di Padova, E. N. Olson, R. J. Ulevitch, and J. Han. 1999. Regulation of the MEF2 family of transcription factors by p38. Mol. Cell. Biol. 19:21–30.
   PubMedGoogle Scholar