Biology:Myogenin
Generic protein structure example |
Myogenin, is a transcriptional activator encoded by the MYOG gene.[1] 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.[2][3]
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
- ↑ "MYOG - Myogenin - Homo sapiens (Human) - MYOG gene & protein" (in en). https://www.uniprot.org/uniprot/P15173.
- ↑ "Muscle deficiency and neonatal death in mice with a targeted mutation in the myogenin gene". Nature 364 (6437): 501–6. August 1993. doi:10.1038/364501a0. PMID 8393145. Bibcode: 1993Natur.364..501H.
- ↑ "Myogenin gene disruption results in perinatal lethality because of severe muscle defect". Nature 364 (6437): 532–5. August 1993. doi:10.1038/364532a0. PMID 8393146. Bibcode: 1993Natur.364..532N.
- ↑ "I-mf, a novel myogenic repressor, interacts with members of the MyoD family". Cell 86 (5): 731–41. September 1996. doi:10.1016/s0092-8674(00)80148-8. PMID 8797820.
- ↑ "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. October 2002. doi:10.1096/fj.02-0123fje. PMID 12207009.
- ↑ 6.0 6.1 "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. April 1999. doi:10.1128/MCB.19.4.2577. PMID 10082523.
- ↑ "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. March 1996. doi:10.1074/jbc.271.9.5258. PMID 8617811.
- ↑ "Differential interactions of Id proteins with basic-helix-loop-helix transcription factors". The Journal of Biological Chemistry 272 (32): 19785–93. August 1997. doi:10.1074/jbc.272.32.19785. PMID 9242638.
- ↑ "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. September 1992. doi:10.1016/S0021-9258(19)37069-3. PMID 1325437.
Further reading
- "The myoD gene family: nodal point during specification of the muscle cell lineage". Science 251 (4995): 761–6. February 1991. doi:10.1126/science.1846704. PMID 1846704. Bibcode: 1991Sci...251..761W.
- "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. September 1992. doi:10.1016/S0021-9258(19)37069-3. PMID 1325437.
- "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. October 1992. doi:10.1073/pnas.89.20.9484. PMID 1329097. Bibcode: 1992PNAS...89.9484F.
- "Functional activity of myogenic HLH proteins requires hetero-oligomerization with E12/E47-like proteins in vivo". Cell 66 (2): 305–15. July 1991. doi:10.1016/0092-8674(91)90620-E. PMID 1649701.
- "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. November 1991. doi:10.1083/jcb.115.4.905. PMID 1659574.
- "Human MyoD: cDNA and deduced amino acid sequence". Nucleic Acids Research 19 (5): 1148. March 1991. doi:10.1093/nar/19.5.1148. PMID 1850513.
- "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. November 1990. doi:10.1016/0888-7543(90)90028-S. PMID 1962752.
- "Myogenin resides in the nucleus and acquires high affinity for a conserved enhancer element on heterodimerization". Genes & Development 4 (4): 582–95. April 1990. doi:10.1101/gad.4.4.582. PMID 2163343.
- "Differential expression of myogenic determination genes in muscle cells: possible autoactivation by the Myf gene products". The EMBO Journal 8 (12): 3617–25. December 1989. doi:10.1002/j.1460-2075.1989.tb08535.x. PMID 2583111.
- "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. March 1996. doi:10.1074/jbc.271.9.5258. PMID 8617811.
- "I-mf, a novel myogenic repressor, interacts with members of the MyoD family". Cell 86 (5): 731–41. September 1996. doi:10.1016/S0092-8674(00)80148-8. PMID 8797820.
- "Muscle LIM protein promotes myogenesis by enhancing the activity of MyoD". Molecular and Cellular Biology 17 (8): 4750–60. August 1997. doi:10.1128/mcb.17.8.4750. PMID 9234731.
- "Differential interactions of Id proteins with basic-helix-loop-helix transcription factors". The Journal of Biological Chemistry 272 (32): 19785–93. August 1997. doi:10.1074/jbc.272.32.19785. PMID 9242638.
- "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. April 1999. doi:10.1128/MCB.19.4.2577. PMID 10082523.
- "Human bHLH transcription factor gene myogenin (MYOG): genomic sequence and negative mutation analysis in patients with severe congenital myopathies". Genomics 57 (3): 419–23. May 1999. doi:10.1006/geno.1998.5719. PMID 10329008.
- "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. September 1999. doi:10.1093/nar/27.18.3752. PMID 10471746.
- "A novel type of calmodulin interaction in the inhibition of basic helix-loop-helix transcription factors". Biochemistry 39 (15): 4366–74. April 2000. doi:10.1021/bi992533u. PMID 10757985.
- "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. October 2002. doi:10.1096/fj.02-0123fje. PMID 12207009.
External links
- Myogenin at the US National Library of Medicine Medical Subject Headings (MeSH)
Original source: https://en.wikipedia.org/wiki/Myogenin.
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