MyoD

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Myogenic differentiation 1

PDB rendering based on 1mdy.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
SymbolsMYOD1; MYF3; MYOD; PUM; bHLHc1
External IDsOMIM: 159970 MGI: 97275 HomoloGene: 7857 GeneCards: MYOD1 Gene
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez465417927
EnsemblENSG00000129152ENSMUSG00000009471
UniProtP15172P10085
RefSeq (mRNA)NM_002478NM_010866
RefSeq (protein)NP_002469NP_034996
Location (UCSC)Chr 11:
17.74 – 17.74 Mb		Chr 7:
46.38 – 46.38 Mb
PubMed search
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MyoD is a protein with a key role in regulating muscle differentiation. MyoD belongs to a family of proteins known as myogenic regulatory factors (MRFs).[1] These bHLH (basic helix loop helix) transcription factors act sequentially in myogenic differentiation. MRF family members include MyoD, Myf5, myogenin, and MRF4 (Myf6).

MyoD is one of the earliest markers of myogenic commitment. MyoD is expressed in activated satellite cells, but not in quiescent satellite cells. Although MyoD marks myoblast commitment, muscle development is not dramatically ablated in mouse mutants lacking the MyoD gene. This is likely to be due to functional redundancy from Myf5. Nevertheless, the combination of MyoD and Myf5 is vital to the success of myogenesis.

Functions of MyoD

The function of MyoD in development is to commit mesoderm cells to a skeletal lineage, and then to regulate that process. MyoD may also play a role in regulating muscle repair. MyoD mRNA levels are also reported to be elevated in aging skeletal muscle.

One of the main actions of MyoD is to remove cells from the cell cycle (halt proliferation) by enhancing the transcription of p21. MyoD is inhibited by cyclin dependent kinases (CDKs). CDKs are in turn inhibited by p21. Thus MyoD enhances its own activity in the cell.

Interactions

MyoD has been shown to interact with HDAC1,[2][3] ID1,[4][5][6][7][8][9] ID2,[5] Retinoblastoma protein,[3][10] STAT3,[11] CSRP3,[12] Cyclin-dependent kinase 4,[13][14] CREB-binding protein,[15][16] TCF3,[5][17] MOS,[18] EP300,[16][19] C-jun,[20] Cyclin-dependent kinase inhibitor 1C,[21] Retinoid X receptor alpha[22] and MDFI.[23]

Coactivators of MyoD

IFRD1 is a positive cofactor of MyoD, as it cooperates with MyoD at inducing the transcriptional activity of MEF2C (by displacing HDAC4 from MEF2C); moreover IFRD1 also represses the transcriptional activity of NF-κB, which is known to inhibit MyoD mRNA accumulation.[24][25]

References

  1. ↑ "Entrez Gene: MYOD1 myogenic differentiation 1". 
  2. ↑ Puri, P L; Iezzi S, Stiegler P, Chen T T, Schiltz R L, Muscat G E, Giordano A, Kedes L, Wang J Y, Sartorelli V (October 2001). "Class I histone deacetylases sequentially interact with MyoD and pRb during skeletal myogenesis". Mol. Cell (United States) 8 (4): 885–97. doi:10.1016/S1097-2765(01)00373-2. ISSN 1097-2765. PMID 11684023.  Unknown parameter |unused_data= ignored (help);
  3. ↑ 3.0 3.1 Mal, A; Sturniolo M, Schiltz R L, Ghosh M K, Harter M L (April 2001). "A role for histone deacetylase HDAC1 in modulating the transcriptional activity of MyoD: inhibition of the myogenic program". EMBO J. (England) 20 (7): 1739–53. doi:10.1093/emboj/20.7.1739. ISSN 0261-4189. PMC 145490. PMID 11285237. 
  4. ↑ Garkavtsev, Igor; Kozin Sergey V, Chernova Olga, Xu Lei, Winkler Frank, Brown Edward, Barnett Gene H, Jain Rakesh K (March 2004). "The candidate tumour suppressor protein ING4 regulates brain tumour growth and angiogenesis". Nature (England) 428 (6980): 328–32. doi:10.1038/nature02329. PMID 15029197. 
  5. ↑ 5.0 5.1 5.2 Langlands, K; Yin X, Anand G, Prochownik E V (August 1997). "Differential interactions of Id proteins with basic-helix-loop-helix transcription factors". J. Biol. Chem. (UNITED STATES) 272 (32): 19785–93. doi:10.1074/jbc.272.32.19785. ISSN 0021-9258. PMID 9242638. 
  6. ↑ Finkel, T; Duc J, Fearon E R, Dang C V, Tomaselli G F (January 1993). "Detection and modulation in vivo of helix-loop-helix protein-protein interactions". J. Biol. Chem. (UNITED STATES) 268 (1): 5–8. ISSN 0021-9258. PMID 8380166. 
  7. ↑ Gupta, K; Anand G, Yin X, Grove L, Prochownik E V (March 1998). "Mmip1: a novel leucine zipper protein that reverses the suppressive effects of Mad family members on c-myc". Oncogene (ENGLAND) 16 (9): 1149–59. doi:10.1038/sj.onc.1201634. ISSN 0950-9232. PMID 9528857. 
  8. ↑ McLoughlin, Patricia; Ehler Elisabeth, Carlile Graeme, Licht Jonathan D, Schäfer Beat W (October 2002). "The LIM-only protein DRAL/FHL2 interacts with and is a corepressor for the promyelocytic leukemia zinc finger protein". J. Biol. Chem. (United States) 277 (40): 37045–53. doi:10.1074/jbc.M203336200. ISSN 0021-9258. PMID 12145280. 
  9. ↑ Ling, Ming-Tat; Chiu Yung-Tuen, Lee Terence Kin Wah, Leung Steve Chin Lung, Fung Maggie Ka Lai, Wang Xianghong, Wong Kwong Fai, Wong Yong-Chuan (September 2008). "Id-1 induces proteasome-dependent degradation of the HBX protein". J. Mol. Biol. (England) 382 (1): 34–43. doi:10.1016/j.jmb.2007.06.020. PMID 18674781. 
  10. ↑ Gu, W; Schneider J W, Condorelli G, Kaushal S, Mahdavi V, Nadal-Ginard B (February 1993). "Interaction of myogenic factors and the retinoblastoma protein mediates muscle cell commitment and differentiation". Cell (UNITED STATES) 72 (3): 309–24. doi:10.1016/0092-8674(93)90110-C. ISSN 0092-8674. PMID 8381715. 
  11. ↑ Kataoka, Yoshihisa; Matsumura Itaru, Ezoe Sachiko, Nakata Soichi, Takigawa Eri, Sato Yusuke, Kawasaki Akira, Yokota Takashi, Nakajima Koichi, Felsani Armando, Kanakura Yuzuru (November 2003). "Reciprocal inhibition between MyoD and STAT3 in the regulation of growth and differentiation of myoblasts". J. Biol. Chem. (United States) 278 (45): 44178–87. doi:10.1074/jbc.M304884200. ISSN 0021-9258. PMID 12947115. 
  12. ↑ Kong, Y; Flick M J, Kudla A J, Konieczny S F (August 1997). "Muscle LIM protein promotes myogenesis by enhancing the activity of MyoD". Mol. Cell. Biol. (UNITED STATES) 17 (8): 4750–60. ISSN 0270-7306. PMC 232327. PMID 9234731. 
  13. ↑ Zhang, J M; Zhao X, Wei Q, Paterson B M (December 1999). "Direct inhibition of G(1) cdk kinase activity by MyoD promotes myoblast cell cycle withdrawal and terminal differentiation". EMBO J. (ENGLAND) 18 (24): 6983–93. doi:10.1093/emboj/18.24.6983. ISSN 0261-4189. PMC 1171761. PMID 10601020. 
  14. ↑ Zhang, J M; Wei Q, Zhao X, Paterson B M (February 1999). "Coupling of the cell cycle and myogenesis through the cyclin D1-dependent interaction of MyoD with cdk4". EMBO J. (ENGLAND) 18 (4): 926–33. doi:10.1093/emboj/18.4.926. ISSN 0261-4189. PMC 1171185. PMID 10022835. 
  15. ↑ Polesskaya, A; Naguibneva I, Duquet A, Bengal E, Robin P, Harel-Bellan A (August 2001). "Interaction between acetylated MyoD and the bromodomain of CBP and/or p300". Mol. Cell. Biol. (United States) 21 (16): 5312–20. doi:10.1128/MCB.21.16.5312-5320.2001. ISSN 0270-7306. PMC 87255. PMID 11463815. 
  16. ↑ 16.0 16.1 Sartorelli, V; Huang J, Hamamori Y, Kedes L (February 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. (UNITED STATES) 17 (2): 1010–26. ISSN 0270-7306. PMC 231826. PMID 9001254. 
  17. ↑ Maleki, S J; Royer C A, Hurlburt B K (June 1997). "MyoD-E12 heterodimers and MyoD-MyoD homodimers are equally stable". Biochemistry (UNITED STATES) 36 (22): 6762–7. doi:10.1021/bi970262m. ISSN 0006-2960. PMID 9184158. 
  18. ↑ Lenormand, J L; Benayoun B, Guillier M, Vandromme M, Leibovitch M P, Leibovitch S A (February 1997). "Mos activates myogenic differentiation by promoting heterodimerization of MyoD and E12 proteins". Mol. Cell. Biol. (UNITED STATES) 17 (2): 584–93. ISSN 0270-7306. PMC 231783. PMID 9001211. 
  19. ↑ Lau, P; Bailey P, Dowhan D H, Muscat G E (January 1999). "Exogenous expression of a dominant negative RORalpha1 vector in muscle cells impairs differentiation: RORalpha1 directly interacts with p300 and myoD". Nucleic Acids Res. (ENGLAND) 27 (2): 411–20. doi:10.1093/nar/27.2.411. ISSN 0305-1048. PMC 148194. PMID 9862959. 
  20. ↑ Bengal, E; Ransone L, Scharfmann R, Dwarki V J, Tapscott S J, Weintraub H, Verma I M (February 1992). "Functional antagonism between c-Jun and MyoD proteins: a direct physical association". Cell (UNITED STATES) 68 (3): 507–19. doi:10.1016/0092-8674(92)90187-H. ISSN 0092-8674. PMID 1310896. 
  21. ↑ Reynaud, E G; Leibovitch M P, Tintignac L A, Pelpel K, Guillier M, Leibovitch S A (June 2000). "Stabilization of MyoD by direct binding to p57(Kip2)". J. Biol. Chem. (UNITED STATES) 275 (25): 18767–76. doi:10.1074/jbc.M907412199. ISSN 0021-9258. PMID 10764802. 
  22. ↑ Froeschlé, A; Alric S, Kitzmann M, Carnac G, Auradé F, Rochette-Egly C, Bonnieu A (July 1998). "Retinoic acid receptors and muscle b-HLH proteins: partners in retinoid-induced myogenesis". Oncogene (ENGLAND) 16 (26): 3369–78. doi:10.1038/sj.onc.1201894. ISSN 0950-9232. PMID 9692544. 
  23. ↑ Chen, C M; Kraut N, Groudine M, Weintraub H (September 1996). "I-mf, a novel myogenic repressor, interacts with members of the MyoD family". Cell (UNITED STATES) 86 (5): 731–41. doi:10.1016/S0092-8674(00)80148-8. ISSN 0092-8674. PMID 8797820. 
  24. ↑ Micheli L, Leonardi L, Conti F, Buanne P, Canu N, Caruso M, Tirone F (March 2005). "PC4 coactivates MyoD by relieving the histone deacetylase 4-mediated inhibition of myocyte enhancer factor 2C". Mol. Cell. Biol. 25 (6): 2242–59. doi:10.1128/MCB.25.6.2242-2259.2005. PMC 1061592. PMID 15743821. 
  25. ↑ Micheli L, Leonardi L, Conti F, Maresca G, Colazingari S, Mattei E, Lira SA, Farioli-Vecchioli S, Caruso M, Tirone F (February 2011). "PC4/Tis7/IFRD1 stimulates skeletal muscle regeneration and is involved in myoblast differentiation as a regulator of MyoD and NF-kappaB". J. Biol. Chem. 286 (7): 5691–707. doi:10.1074/jbc.M110.162842. PMC 3037682. PMID 21127072. 

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