Myogenin

Myogenin (myogenic factor 4), also known as MYOG, is a gene.[5]

MYOG
Identifiers
Aliases	MYOG, MYF4, bHLHc3, myf-4, myogenin (myogenic factor 4), myogenin
External IDs	OMIM: 159980 MGI: 97276 HomoloGene: 1854 GeneCards: MYOG
Gene location (Human) Chr. Chromosome 1 (human)[1] Band 1q32.1 Start 203,083,129 bp[1] End 203,086,012 bp[1]
Gene location (Mouse) Chr. Chromosome 1 (mouse)[2] Band 1 E4|1 58.18 cM Start 134,289,989 bp[2] End 134,292,548 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • sequence-specific DNA binding • DNA binding • RNA polymerase II regulatory region sequence-specific DNA binding • protein dimerization activity • GO:0001131, GO:0001151, GO:0001130, GO:0001204 DNA-binding transcription factor activity • GO:0001077, GO:0001212, GO:0001213, GO:0001211, GO:0001205 DNA-binding transcription activator activity, RNA polymerase II-specific • GO:0001158 core promoter proximal region sequence-specific DNA binding • GO:0000980 RNA polymerase II cis-regulatory region sequence-specific DNA binding • E-box binding • GO:0001948 protein binding • protein heterodimerization activity • transcription factor activity, RNA polymerase II distal enhancer sequence-specific binding • chromatin DNA binding • GO:0001200, GO:0001133, GO:0001201 DNA-binding transcription factor activity, RNA polymerase II-specific Cellular component • transcription factor complex • protein-DNA complex • cell nucleus • nucleoplasm 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 • cellular response to tumor necrosis factor Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	4656	17928
Ensembl	ENSG00000122180	ENSMUSG00000026459
UniProt	P15173	P12979
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	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

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.[6][7]

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

Interactions

Myogenin has been shown to interact with:

• MDFI,[8]
• POLR2C,[9]
• Serum response factor[10][11]
• Sp1 transcription factor,[10] and
• TCF3.[12][13]

References

1. GRCh38: Ensembl release 89: ENSG00000122180 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000026459 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. "Entrez Gene: MYOG myogenin (myogenic factor 4)".
6. 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. Bibcode:1993Natur.364..501H. doi:10.1038/364501a0. PMID 8393145.
7. 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. Bibcode:1993Natur.364..532N. doi:10.1038/364532a0. PMID 8393146.
8. 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. doi:10.1016/s0092-8674(00)80148-8. PMID 8797820.
9. 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. doi:10.1096/fj.02-0123fje. PMID 12207009.
10. 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. doi:10.1128/MCB.19.4.2577. PMC 84050. PMID 10082523.
11. 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. doi:10.1074/jbc.271.9.5258. PMID 8617811.
12. 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. doi:10.1074/jbc.272.32.19785. PMID 9242638.
13. 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

• Weintraub H, Davis R, Tapscott S, Thayer M, Krause M, Benezra R, Blackwell TK, Turner D, Rupp R, Hollenberg S (February 1991). "The myoD gene family: nodal point during specification of the muscle cell lineage". Science. 251 (4995): 761–6. Bibcode:1991Sci...251..761W. doi:10.1126/science.1846704. PMID 1846704.
• 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.
• Funk WD, Wright WE (October 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". Proceedings of the National Academy of Sciences of the United States of America. 89 (20): 9484–8. Bibcode:1992PNAS...89.9484F. 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 (July 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 (November 1991). "Transcription of the muscle regulatory gene Myf4 is regulated by serum components, peptide growth factors and signaling pathways involving G proteins". The Journal of Cell Biology. 115 (4): 905–17. doi:10.1083/jcb.115.4.905. PMC 2289955. PMID 1659574.
• Pearson-White SH (March 1991). "Human MyoD: cDNA and deduced amino acid sequence". Nucleic Acids Research. 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 (November 1990). "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 (April 1990). "Myogenin resides in the nucleus and acquires high affinity for a conserved enhancer element on heterodimerization". Genes & Development. 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 (December 1989). "Differential expression of myogenic determination genes in muscle cells: possible autoactivation by the Myf gene products". The EMBO Journal. 8 (12): 3617–25. doi:10.1002/j.1460-2075.1989.tb08535.x. PMC 402043. PMID 2583111.
• 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. doi:10.1074/jbc.271.9.5258. PMID 8617811.
• 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. doi:10.1016/S0092-8674(00)80148-8. PMID 8797820.
• Kong Y, Flick MJ, Kudla AJ, Konieczny SF (August 1997). "Muscle LIM protein promotes myogenesis by enhancing the activity of MyoD". Molecular and Cellular Biology. 17 (8): 4750–60. doi:10.1128/mcb.17.8.4750. PMC 232327. PMID 9234731.
• 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. doi:10.1074/jbc.272.32.19785. PMID 9242638.
• 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. doi:10.1128/MCB.19.4.2577. PMC 84050. PMID 10082523.
• Tseng BS, Cavin ST, Hoffman EP, Iannaccone ST, Mancias P, Booth FW, Butler IJ (May 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 (September 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 Research. 27 (18): 3752–61. doi:10.1093/nar/27.18.3752. PMC 148632. PMID 10471746.
• Onions J, Hermann S, Grundström T (April 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 (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. doi:10.1096/fj.02-0123fje. PMID 12207009.

External links

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