MEF2: A transcriptional target for signaling pathways controlling skeletal muscle growth and differentiation

Current Opinion in Cell Biology

Volumn 11, Issue 6, 1999, Pages 683-688

  Naya, Francisco J ^a   Olson, Eric ^a  

^a UNIVERSITY OF TEXAS SOUTHWESTERN MEDICAL CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

TRANSCRIPTION FACTOR;

CELL CYCLE; MESODERM; MUSCLE DEVELOPMENT; MUSCLE GROWTH; MYOBLAST; NONHUMAN; PRIORITY JOURNAL; PROTEIN PHOSPHORYLATION; REVIEW; SIGNAL TRANSDUCTION; SKELETAL MUSCLE; STEM CELL; TISSUE DIFFERENTIATION; TRANSCRIPTION REGULATION;

EUKARYOTA; UNIDENTIFIED BACTERIOPHAGE;

EID: 0032705145     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0955-0674(99)00036-8     Document Type: Review

References (32)

1. Arnold H.-H., Winter B. Muscle differentiation: more complexity to the network of myogenic regulators. Curr Opin Genet Dev. 8:1998;539-544.
2. Currie P.D., Ingham P.W. The generation and interpretation of positional information within the vertebrate myotome. Mech Dev. 73:1998;3-21.
3. Black B.L., Olson E.N. Transcriptional control of muscle development by myocyte enhancer factor-2 (MEF2) proteins. Annu Rev Cell Dev Biol. 14:1998;167-196.
4. Black B.L., Molkentin J.D., Olson E.N. Multiple roles for the MyoD basic region in transmission of transcriptional activation signals and interaction with MEF2. Mol Cell Biol. 18:1998;69-77. This paper shows that MyoD mutants defective in muscle gene activation retain the ability to interact with MEF2. Thus, formation of a myogenic bHLH-MEF2 complex is insufficient to activate myogenesis. The results also demonstrate that the MyoD basic region is required for transmission of an activation signal in conjunction with MEF2. The essential role of the MyoD basic region for transcriptional activation can be bypassed by fusion of MyoD or MEF2 to VP16, but VP16 mutants lacking the MyoD basic region can only activate artificial reporter genes, not endogenous muscle genes.
5. Gerber A.N., Klessert T.R., Bergstrom D.A., Tapscott S.J. Two domains of MyoD mediate transcriptional activation of genes in repressive chromatin: a mechanism for lineage determination in myogenesis. Genes Dev. 11:1997;436-450.
6. Puri P.L., Sartorelli V., Yang X.J., Hamamori Y., Ogryzko V.V., Howard B.H., Kedes L., Wang J.Y., Graessmann A., Nakatani Y., Levrero M. Differential roles of p300 and PCAF histone acetyltransferases in muscle differentiation. Mol Cell. 1:1997;35-45.
7. Bailey P., Sartorelli V., Hamamori Y., Muscat G.E. The orphan nuclear receptor, COUP-TF I.I., inhibits myogenesis by post-transcriptional regulation of MyoD function: COUP-TF II directly interacts with p300 and MyoD. Nucleic Acids Res. 23:1998;5501-5510.
8. Bailey P., Downes M., Lau P., Harris J., Chen S.L., Hamamori Y., Sartorelli V., Muscat G.E. The nuclear receptor corepressor N-CoR regulates differentiation: N-CoR directly interacts with MyoD. Mol Endocrinol. 13:1999;1155-1168.
9. Grayson J., Bassel-Buby R., Williams R.S. Collaborative interactions between MEF-2 and Sp1 in muscle-specific gene interaction. J Cell Biochem. 70:1998;366-375.
10. Kraine D., Bai G., Okamoto S., Carles M., Kusiak J.W., Brent R.N., Lipton S.A. Synergistic activation of the N-methyl-D-aspartate receptor subunit 1 promoter by myocyte enhancer factor 2C and Sp1. J Biol Chem. 273:1998;26218-26224.
11. Lakich M.M., Diagana T.T., North D.L., Whalen R.G. MEF-2 and Oct-1 bind to two homologous promoter sequence elements and participate in the expression of a skeletal muscle-specific gene. J Biol Chem. 273:1998;15217-15226.
12. Naya F.J., Wu C., Richardson J.A., Overbeek P., Olson E.N. Transcriptional activity of MEF2 during mouse embryogenesis monitored with a MEF2-dependent transgene. Development. 126:1999;2045-2052. This paper describes a method for identifying transcriptionally active MEF2 proteins in vivo, using a MEF2-dependent lacZ reporter gene. Consistent with the important role of MEF2 proteins in muscle development, a MEF2-dependent lacZ reporter gene is shown to be expressed at high levels in skeletal, cardiac and smooth muscle cells during embryogenesis. Suprisingly, however, this transgene is down-regulated to basal levels in muscle cells after birth, despite the presence of high levels of MEF2 protein. These findings suggest that MEF2 protein is inactivated through a post-translational mechanism after birth.
13. De Angelis L., Borghi S., Melchionna R., Berghella L., Baccarani Contri M., Parise F., Ferrari S., Cossu G. Inhibition of myogenesis by transforming growth factor β is density-dependent and related to the translocation of transcription factor MEF2 to the cytoplasm. Proc Natl Acad Sci USA. 95:1998;12358-12363. This paper describes a novel mechanism for inhibition of MEF2 activity by sequestration in the cytoplasm in response to TGF-β-signaling. The results may explain how TGF-β blocks myogenesis, under certain conditions, without affecting the DNA-binding activity of MyoD. TGF-β-mediated inhibition of nuclear translocation of MEF2 can be bypassed by introducing a SV40 nuclear localization signal.
14. Wilson-Rawls J., Molkentin J., Black B., Olson E. Activated Notch inhibits myogenic activity of the MADS-box transcription factor myocyte enhancer factor 2C. Mol Cell Biol. 19:1999;2853-2862.
15. Bennet A.M., Tonks N.K. Regulation of distinct stages of skeletal muscle differentiation by mitogen-activated protein kinases. Science. 278:1997;1288-1291.
16. Zetser A., Gredinger E., Bengal E. p38 mitogen-activated protein kinase pathway promotes skeletal muscle differentiation. J Biol Chem. 274:1999;5193-5200.
17. Han J., Jiang Y., Li Z., Kravchenko V.V., Ulevitch R.J. Activation of the transcription factor MEF2C by the MAP kinase p38 in inflammation. Nature. 386:1997;296-299.
18. Kato Y., Kravchenko V.V., Tapping R.I., Han J., Ulevitch R.J., Lee J.-D. BMK1/ERK5 regulates serum-induced early gene expression through transcription factor MEF2C. EMBO J. 16:1997;7054-7066.
19. Zhao M., New L., Kravchenko V.V., Kat Y., Gram H., Di Padova F., Olson E.N., Ulevitch R.J., Han J. Regulation of the MEF2 family of transcription factors by p38. Mol Cell Biol. 19:1999;21-30.
20. Yang C.-C., Ornatsky O., McDermott J.C., Cruz T.F., Prody C.A. Interaction of myocyte enhancer factor 2 (MEF2) with a mitogen-activated protein kinase, ERK5/BMK1. Nucleic Acids Res. 26:1998;4771-4777.
21. Clarke N., Arenzana N., Hai T., Minden A., Prywes R. Epidermal growth factor induction of the c-jun promoter by a rac pathway. Mol Cell Biol. 18:1998;1065-1073.
22. Ornatsky O.I., Cox D.M., Tangirala P., Andreucci J.J., Quinn Z.A., Wrana J.L., Prywes R., Yu Y.-T., McDermott J.C. Post-translational control of the MEF2A transcriptional regulatory protein. Nucleic Acids Res. 27:1999;2646-2654.
23. 2-terminal kinase, p38s, and extracellular signal-regulated kinase 5. Mol Cell Biol. 19:1999;4289-4301.
24. Yang S., Galanis A., Sharrocks A.D. Targeting of p38 mitogen activated protein kinases to MEF2 transcription factors. Mol Cell Biol. 19:1999;4028-4038. This paper identifies specific docking sites in MEF2A and MEF2C for the p38 subfamily members p38a and p38β2. The kinase-docking domain (D-domain) from MEF2A is also shown to be sufficient to confer p38 responsiveness on other transcription factors. These findings provide a mechanism to account for selective activation of different MEF2 isoforms by different MAP kinases.
25. Walsh K., Perlman H. Cell cycle exit upon myogenic differentiation. Curr Opin Genet Dev. 7:1997;597-602.
26. 2 phases of the cell cycle. J Cell Biol. 135:1996;441-456.
27. Sellers W.R., Novitch B.G., Miyake S., Heith A., Otterson G.A., Kaye F.J., Lassar A.B., Kaelin W.G. Jr. Stable binding to E2F is not required for the retinoblastoma protein to activate transcription, promote differentiation, and suppress tumor cell growth. Genes Dev. 12:1998;95-106.
28. KIP2 act in parallel with myogenin at an early step in the myogenic pathway.
29. Novitch B.G., Spicer D.B., Kim P.S., Cheung W.L., Lassar A.B. pRb is required for MEF2-dependent gene expression as well as cell-cycle arrest during skeletal muscle differentiation. Curr Biol. 9:1999;449-459. This interesting paper demonstrates a role for MyoD and Rb in the control of MEF2 function. MyoD and Rb appear to regulate phosphorylation-dependent activation of MEF2C on the basis of the requirement of Ser387 for their effect. This study provides an explanation for the differentiation-defective phenotype of Rb mutant myoblasts.
30. Chin E., Olson E.N., Yang Q., Shelton J., Bassel-Duby R., Williams R.S. A calcineurin dependent transcriptional pathway controls skeletal muscle fiber type. Genes Dev. 12:1998;2499-2509. This study reveals a novel role for calcineurin in the control of slow-fiber gene expression. The study shows that a slow-muscle regulatory element from the myoglobin gene contains adjacent NFAT- and MEF2-binding sites and implicates these sites in slow-fiber gene expression. The study also demonstrates that systemic delivery of cyclosporin A in vivo can evoke a slow to fast fiber transition, consistent with a requisite role for calcineurin in slow-fiber gene expression.
31. Calvo S., Venepally P., Cheng J., Bounanno A. Fiber-type specific transcription of the troponin I slow gene is regulated by multiple elelments. Mol Cell Biol. 19:1999;515-525.
32. Esser K., Nelson T., Lupa-Kimball V., Blough G.E. The CACC box and myocyte enhancer factor-2 sites within the myosin light chain 2 slow promoter cooperate in regulating nerve-specific transcription in skeletal muscle. J Biol Chem. 274:1999;12095-12102.