Myogenin

MYOG
Identifiers
Aliases	MYOG, MYF4, bHLHc3, myf-4, myogenin (myogenic factor 4)
External IDs	OMIM: 159980 MGI: 97276 HomoloGene: 1854 GeneCards: MYOG
Gene ontology Molecular function • sequence-specific DNA binding • DNA binding • RNA polymerase II regulatory region sequence-specific DNA binding • protein dimerization activity • core promoter binding • transcription factor activity, sequence-specific DNA binding • transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding • transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding • core promoter proximal region sequence-specific DNA binding • RNA polymerase II core promoter proximal region sequence-specific DNA binding • E-box binding • protein binding • protein heterodimerization activity • transcription factor activity, RNA polymerase II distal enhancer sequence-specific binding • chromatin DNA binding Cellular component • transcription factor complex • nucleoplasm • protein-DNA complex • nucleus Biological process • cellular response to retinoic acid • positive regulation of myotube differentiation • cell differentiation • myotube differentiation • negative regulation of glycolytic process • regulation of transcription, DNA-templated • cellular response to lithium ion • ossification • positive regulation of muscle cell differentiation • response to muscle activity involved in regulation of muscle adaptation • muscle cell fate commitment • cellular response to growth factor stimulus • cellular response to estradiol stimulus • positive regulation of oxidative phosphorylation • muscle organ development • striated muscle atrophy • mRNA transcription from RNA polymerase II promoter • cellular response to magnetism • positive regulation of skeletal muscle fiber development • transcription, DNA-templated • multicellular organism development • positive regulation of transcription, DNA-templated • response to gravity • positive regulation of myoblast fusion • positive regulation of muscle atrophy • skeletal muscle tissue regeneration • positive regulation of myoblast differentiation • skeletal muscle fiber development • response to electrical stimulus involved in regulation of muscle adaptation • skeletal muscle atrophy • skeletal muscle cell differentiation • response to denervation involved in regulation of muscle adaptation • cell cycle • regulation of myoblast fusion • myoblast differentiation • regulation of skeletal muscle satellite cell proliferation • skeletal muscle tissue development • response to muscle activity • positive regulation of transcription from RNA polymerase II promoter • negative regulation of cell proliferation • positive regulation of cell cycle arrest Sources:Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	4656	17928
Ensembl	ENSG00000122180	ENSMUSG00000026459
UniProt	P15173	P12979
RefSeq (mRNA)	NM_002479	NM_031189
RefSeq (protein)	NP_002470.2	NP_112466.1
Location (UCSC)	Chr 1: 203.08 – 203.09 Mb	Chr 1: 134.29 – 134.29 Mb
PubMed search	[1]	[2]
Wikidata

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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 fusion of myogenic precursor cells to either new or previously existing fibers during the process of differentiation in 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.

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

Interactions

Myogenin has been shown to interact with:

• MDFI,^[4]
• POLR2C,^[5]
• Serum response factor^[6][7]
• Sp1 transcription factor,^[6] and
• TCF3.^[8][9]

References

1. "Human PubMed Reference:".
2. "Mouse PubMed Reference:".
3. "Entrez Gene: MYOG myogenin (myogenic factor 4)".
4. Chen CM, Kraut N, Groudine M, Weintraub H (Sep 1996). "I-mf, a novel myogenic repressor, interacts with members of the MyoD family". Cell. 86 (5): 731–41. doi:10.1016/s0092-8674(00)80148-8. PMID 8797820.
5. Corbi N, Di Padova M, De Angelis R, Bruno T, Libri V, Iezzi S, Floridi A, Fanciulli M, Passananti C (Oct 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 J. 16 (12): 1639–41. doi:10.1096/fj.02-0123fje. PMID 12207009.
6. Biesiada E, Hamamori Y, Kedes L, Sartorelli V (Apr 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". Mol. Cell. Biol. 19 (4): 2577–84. PMC 84050. PMID 10082523.
7. Groisman R, Masutani H, Leibovitch MP, Robin P, Soudant I, Trouche D, Harel-Bellan A (Mar 1996). "Physical interaction between the mitogen-responsive serum response factor and myogenic basic-helix-loop-helix proteins". J. Biol. Chem. 271 (9): 5258–64. doi:10.1074/jbc.271.9.5258. PMID 8617811.
8. Langlands K, Yin X, Anand G, Prochownik EV (Aug 1997). "Differential interactions of Id proteins with basic-helix-loop-helix transcription factors". J. Biol. Chem. 272 (32): 19785–93. doi:10.1074/jbc.272.32.19785. PMID 9242638.
9. Chakraborty T, Martin JF, Olson EN (Sep 1992). "Analysis of the oligomerization of myogenin and E2A products in vivo using a two-hybrid assay system". J. Biol. Chem. 267 (25): 17498–501. PMID 1325437.

Further reading

• Weintraub H, Davis R, Tapscott S, Thayer M, Krause M, Benezra R, Blackwell TK, Turner D, Rupp R, Hollenberg S (1991). "The myoD gene family: nodal point during specification of the muscle cell lineage.". Science. 251 (4995): 761–6. doi:10.1126/science.1846704. PMID 1846704.
• Chakraborty T, Martin JF, Olson EN (1992). "Analysis of the oligomerization of myogenin and E2A products in vivo using a two-hybrid assay system.". J. Biol. Chem. 267 (25): 17498–501. PMID 1325437.
• Funk WD, Wright WE (1992). "Cyclic amplification and selection of targets for multicomponent complexes: myogenin interacts with factors recognizing binding sites for basic helix-loop-helix, nuclear factor 1, myocyte-specific enhancer-binding factor 2, and COMP1 factor.". Proc. Natl. Acad. Sci. U.S.A. 89 (20): 9484–8. doi:10.1073/pnas.89.20.9484. PMC 50156. PMID 1329097.
• Lassar AB, Davis RL, Wright WE, Kadesch T, Murre C, Voronova A, Baltimore D, Weintraub H (1991). "Functional activity of myogenic HLH proteins requires hetero-oligomerization with E12/E47-like proteins in vivo.". Cell. 66 (2): 305–15. doi:10.1016/0092-8674(91)90620-E. PMID 1649701.
• Salminen A, Braun T, Buchberger A, Jürs S, Winter B, Arnold HH (1991). "Transcription of the muscle regulatory gene Myf4 is regulated by serum components, peptide growth factors and signaling pathways involving G proteins.". J. Cell Biol. 115 (4): 905–17. doi:10.1083/jcb.115.4.905. PMC 2289955. PMID 1659574.
• Pearson-White SH (1991). "Human MyoD: cDNA and deduced amino acid sequence.". Nucleic Acids Res. 19 (5): 1148. doi:10.1093/nar/19.5.1148. PMC 333794. PMID 1850513.
• Olson E, Edmondson D, Wright WE, Lin VK, Guenet JL, Simon-Chazottes D, Thompson LH, Stallings RL, Schroeder WT, Duvic M (1991). "Myogenin is in an evolutionarily conserved linkage group on human chromosome 1q31-q41 and unlinked to other mapped muscle regulatory factor genes.". Genomics. 8 (3): 427–34. doi:10.1016/0888-7543(90)90028-S. PMID 1962752.
• Brennan TJ, Olson EN (1990). "Myogenin resides in the nucleus and acquires high affinity for a conserved enhancer element on heterodimerization.". Genes Dev. 4 (4): 582–95. doi:10.1101/gad.4.4.582. PMID 2163343.
• Braun T, Bober E, Buschhausen-Denker G, Kohtz S, Grzeschik KH, Arnold HH, Kotz S (1990). "Differential expression of myogenic determination genes in muscle cells: possible autoactivation by the Myf gene products.". EMBO J. 8 (12): 3617–25. PMC 402043. PMID 2583111.
• Groisman R, Masutani H, Leibovitch MP, Robin P, Soudant I, Trouche D, Harel-Bellan A (1996). "Physical interaction between the mitogen-responsive serum response factor and myogenic basic-helix-loop-helix proteins.". J. Biol. Chem. 271 (9): 5258–64. doi:10.1074/jbc.271.9.5258. PMID 8617811.
• Chen CM, Kraut N, Groudine M, Weintraub H (1996). "I-mf, a novel myogenic repressor, interacts with members of the MyoD family.". Cell. 86 (5): 731–41. doi:10.1016/S0092-8674(00)80148-8. PMID 8797820.
• Kong Y, Flick MJ, Kudla AJ, Konieczny SF (1997). "Muscle LIM protein promotes myogenesis by enhancing the activity of MyoD.". Mol. Cell. Biol. 17 (8): 4750–60. doi:10.1128/mcb.17.8.4750. PMC 232327. PMID 9234731.
• Langlands K, Yin X, Anand G, Prochownik EV (1997). "Differential interactions of Id proteins with basic-helix-loop-helix transcription factors.". J. Biol. Chem. 272 (32): 19785–93. doi:10.1074/jbc.272.32.19785. PMID 9242638.
• Biesiada E, Hamamori Y, Kedes L, Sartorelli V (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.". Mol. Cell. Biol. 19 (4): 2577–84. PMC 84050. PMID 10082523.
• Tseng BS, Cavin ST, Hoffman EP, Iannaccone ST, Mancias P, Booth FW, Butler IJ (1999). "Human bHLH transcription factor gene myogenin (MYOG): genomic sequence and negative mutation analysis in patients with severe congenital myopathies.". Genomics. 57 (3): 419–23. doi:10.1006/geno.1998.5719. PMID 10329008.
• Knoepfler PS, Bergstrom DA, Uetsuki T, Dac-Korytko I, Sun YH, Wright WE, Tapscott SJ, Kamps MP (1999). "A conserved motif N-terminal to the DNA-binding domains of myogenic bHLH transcription factors mediates cooperative DNA binding with pbx-Meis1/Prep1.". Nucleic Acids Res. 27 (18): 3752–61. doi:10.1093/nar/27.18.3752. PMC 148632. PMID 10471746.
• Onions J, Hermann S, Grundström T (2000). "A novel type of calmodulin interaction in the inhibition of basic helix-loop-helix transcription factors.". Biochemistry. 39 (15): 4366–74. doi:10.1021/bi992533u. PMID 10757985.
• Corbi N, Di Padova M, De Angelis R, Bruno T, Libri V, Iezzi S, Floridi A, Fanciulli M, Passananti C (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 J. 16 (12): 1639–41. doi:10.1096/fj.02-0123fje. PMID 12207009.

External links

• Myogenin at the US National Library of Medicine Medical Subject Headings (MeSH)