Myogenin

MYOG
Identifiers
Aliases	MYOG, MYF4, bHLHc3, myf-4, myogenin (myogenic factor 4), myogenin
External IDs	OMIM: 159980; MGI: 97276; HomoloGene: 1854; GeneCards: MYOG; OMA:MYOG - orthologs
Gene location (Human) Chr. Chromosome 1 (human) Band 1q32.1 Start 203,083,129 bp End 203,086,012 bp
Gene location (Mouse) Chr. Chromosome 1 (mouse) Band 1 E4|1 58.18 cM Start 134,217,727 bp End 134,220,286 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in muscle of thigh gastrocnemius muscle glutes triceps brachii muscle Skeletal muscle tissue of rectus abdominis Skeletal muscle tissue of biceps brachii vastus lateralis muscle tibialis anterior muscle jejunum mouth Top expressed in myotome superior surface of tongue internal carotid artery human fetus pineal gland plantaris muscle dermis ankle joint extraocular muscle muscle of thigh More reference expression data BioGPS More reference expression data
Gene ontology Molecular function sequence-specific DNA binding DNA binding RNA polymerase II transcription regulatory region sequence-specific DNA binding protein dimerization activity DNA-binding transcription factor activity DNA-binding transcription activator activity, RNA polymerase II-specific cis-regulatory region sequence-specific DNA binding RNA polymerase II cis-regulatory 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 DNA-binding transcription factor activity, RNA polymerase II-specific Cellular component transcription regulator complex protein-DNA complex 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 by RNA polymerase II 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 by RNA polymerase II negative regulation of cell population proliferation 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: 134.22 – 134.22 Mb PubMed search
Wikidata
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Myogenin, is a transcriptional activator encoded by the MYOG gene. 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.

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

Interactions

Myogenin has been shown to interact with:

• MDFI,
• POLR2C,
• Serum response factor
• Sp1 transcription factor, and
• TCF3.

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. doi:10.1016/S0021-9258(19)37069-3. 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. S2CID 25957022.
• 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. S2CID 16252710.
• 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. S2CID 30243193.

External links

• Myogenin at the U.S. National Library of Medicine Medical Subject Headings (MeSH)