Myogenin

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MYOG
Identifiers
Aliases MYOG, MYF4, bHLHc3, myf-4, myogenin (myogenic factor 4), myogenin
External IDs OMIM: 159980 MGI: 97276 HomoloGene: 1854 GeneCards: MYOG
RNA expression pattern
PBB GE MYOG 207282 s at fs.png
More reference expression data
Orthologs
Species Human Mouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_002479

NM_031189

RefSeq (protein)

NP_002470

NP_112466

Location (UCSC) Chr 1: 203.08 – 203.09 Mb Chr 1: 134.29 – 134.29 Mb
PubMed search [1] [2]
Wikidata
View/Edit Human View/Edit Mouse

Myogenin (myogenic factor 4), also known as MYOG, is a gene.[3]

Myogenin is a muscle-specific basic-helix-loop-helix (bHLH) transcription factor involved in the coordination of skeletal muscle development or myogenesis and repair. Myogenin is a member of the MyoD family of transcription factors, which also includes MyoD, Myf5, and Mrf4.

In mice, myogenin is essential for the development of functional skeletal muscle. Myogenin is required for the proper differentiation of most myogenic precursor cells during the process of myogenesis. When the DNA coding for myogenin was knocked out of the mouse genome, severe skeletal muscle defects were observed. Mice lacking both copies of myogenin (homozygous-null) suffer from perinatal lethality due to the lack of mature secondary skeletal muscle fibers throughout the body.[4][5]

In cell culture, myogenin can induce myogenesis in a variety of non-muscle cell types.

Interactions[edit]

Myogenin has been shown to interact with:

References[edit]

  1. ^ "Human PubMed Reference:". 
  2. ^ "Mouse PubMed Reference:". 
  3. ^ "Entrez Gene: MYOG myogenin (myogenic factor 4)". 
  4. ^ Hasty P, Bradley A, Morris JH, Edmondson DG, Venuti JM, Olson EN, Klein WH (August 1993). "Muscle deficiency and neonatal death in mice with a targeted mutation in the myogenin gene". Nature. 364 (6437): 501–6. PMID 8393145. doi:10.1038/364501a0. 
  5. ^ Nabeshima Y, Hanaoka K, Hayasaka M, Esumi E, Li S, Nonaka I, Nabeshima Y (August 1993). "Myogenin gene disruption results in perinatal lethality because of severe muscle defect". Nature. 364 (6437): 532–5. PMID 8393146. doi:10.1038/364532a0. 
  6. ^ Chen CM, Kraut N, Groudine M, Weintraub H (September 1996). "I-mf, a novel myogenic repressor, interacts with members of the MyoD family". Cell. 86 (5): 731–41. PMID 8797820. doi:10.1016/s0092-8674(00)80148-8. 
  7. ^ Corbi N, Di Padova M, De Angelis R, Bruno T, Libri V, Iezzi S, Floridi A, Fanciulli M, Passananti C (October 2002). "The alpha-like RNA polymerase II core subunit 3 (RPB3) is involved in tissue-specific transcription and muscle differentiation via interaction with the myogenic factor myogenin". FASEB Journal. 16 (12): 1639–41. PMID 12207009. doi:10.1096/fj.02-0123fje. 
  8. ^ a b Biesiada E, Hamamori Y, Kedes L, Sartorelli V (April 1999). "Myogenic basic helix-loop-helix proteins and Sp1 interact as components of a multiprotein transcriptional complex required for activity of the human cardiac alpha-actin promoter". Molecular and Cellular Biology. 19 (4): 2577–84. PMC 84050Freely accessible. PMID 10082523. 
  9. ^ Groisman R, Masutani H, Leibovitch MP, Robin P, Soudant I, Trouche D, Harel-Bellan A (March 1996). "Physical interaction between the mitogen-responsive serum response factor and myogenic basic-helix-loop-helix proteins". The Journal of Biological Chemistry. 271 (9): 5258–64. PMID 8617811. doi:10.1074/jbc.271.9.5258. 
  10. ^ Langlands K, Yin X, Anand G, Prochownik EV (August 1997). "Differential interactions of Id proteins with basic-helix-loop-helix transcription factors". The Journal of Biological Chemistry. 272 (32): 19785–93. PMID 9242638. doi:10.1074/jbc.272.32.19785. 
  11. ^ Chakraborty T, Martin JF, Olson EN (September 1992). "Analysis of the oligomerization of myogenin and E2A products in vivo using a two-hybrid assay system". The Journal of Biological Chemistry. 267 (25): 17498–501. PMID 1325437. 

Further reading[edit]

External links[edit]