- Myogenin
-
Myogenin (myogenic factor 4), also known as MYOG, is a gene.[1]
Myogenin is a muscle-specific basic-helix-loop-helix (bHLH) transcription factor involved in the coordination of skeletal muscle development 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. 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.
Contents
Interactions
Myogenin has been shown to interact with POLR2C,[2] Sp1 transcription factor,[3] TCF3,[4][5] Serum response factor[3][6] and MDFI.[7]
References
- ^ "Entrez Gene: MYOG myogenin (myogenic factor 4)". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4656.
- ^ Corbi, Nicoletta; Di Padova Monica, De Angelis Roberta, Bruno Tiziana, Libri Valentina, Iezzi Simona, Floridi Aristide, Fanciulli Maurizio, Passananti Claudio (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. (United States) 16 (12): 1639–41. doi:10.1096/fj.02-0123fje. PMID 12207009.
- ^ a b 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. (UNITED STATES) 19 (4): 2577–84. ISSN 0270-7306. PMC 84050. PMID 10082523. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=84050.
- ^ Langlands, K; Yin X, Anand G, Prochownik E V (Aug. 1997). "Differential interactions of Id proteins with basic-helix-loop-helix transcription factors". J. Biol. Chem. (UNITED STATES) 272 (32): 19785–93. doi:10.1074/jbc.272.32.19785. ISSN 0021-9258. PMID 9242638.
- ^ Chakraborty, T; Martin J F, Olson E N (Sep. 1992). "Analysis of the oligomerization of myogenin and E2A products in vivo using a two-hybrid assay system". J. Biol. Chem. (UNITED STATES) 267 (25): 17498–501. ISSN 0021-9258. PMID 1325437.
- ^ Groisman, R; Masutani H, Leibovitch M P, 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. (UNITED STATES) 271 (9): 5258–64. doi:10.1074/jbc.271.9.5258. ISSN 0021-9258. PMID 8617811.
- ^ Chen, C M; Kraut N, Groudine M, Weintraub H (Sep. 1996). "I-mf, a novel myogenic repressor, interacts with members of the MyoD family". Cell (UNITED STATES) 86 (5): 731–41. doi:10.1016/S0092-8674(00)80148-8. ISSN 0092-8674. PMID 8797820.
Further reading
- Weintraub H, Davis R, Tapscott S, et al. (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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=50156.
- Lassar AB, Davis RL, Wright WE, et al. (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, et al. (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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2289955.
- 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=333794.
- Olson E, Edmondson D, Wright WE, et al. (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, et al. (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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=402043.
- Groisman R, Masutani H, Leibovitch MP, et al. (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. PMC 232327. PMID 9234731. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=232327.
- 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=84050.
- Tseng BS, Cavin ST, Hoffman EP, et al. (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, et al. (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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=148632.
- 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, et al. (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.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
External links
Transcription factors and intracellular receptors (1) Basic domains (1.1) Basic leucine zipper (bZIP)Activating transcription factor (AATF, 1, 2, 3, 4, 5, 6, 7) · AP-1 (c-Fos, FOSB, FOSL1, FOSL2, JDP2, c-Jun, JUNB, JUND) · BACH (1, 2) · BATF · BLZF1 · C/EBP (α, β, γ, δ, ε, ζ) · CREB (1, 3, L1) · CREM · DBP · DDIT3 · GABPA · HLF · MAF (B, F, G, K) · NFE (2, L1, L2, L3) · NFIL3 · NRL · NRF (1, 2, 3) · XBP1(1.2) Basic helix-loop-helix (bHLH)ATOH1 · AhR · AHRR · ARNT · ASCL1 · BHLHB2 · BMAL (ARNTL, ARNTL2) · CLOCK · EPAS1 · FIGLA · HAND (1, 2) · HES (5, 6) · HEY (1, 2, L) · HES1 · HIF (1A, 3A) · ID (1, 2, 3, 4) · LYL1 · MESP2 · MXD4 · MYCL1 · MYCN · Myogenic regulatory factors (MyoD, Myogenin, MYF5, MYF6) · Neurogenins (1, 2, 3) · NeuroD (1, 2) · NPAS (1, 2, 3) · OLIG (1, 2) · Pho4 · Scleraxis · SIM (1, 2) · TAL (1, 2) · Twist · USF1(1.3) bHLH-ZIP(1.4) NF-1(1.5) RF-X(1.6) Basic helix-span-helix (bHSH)(2) Zinc finger DNA-binding domains (2.1) Nuclear receptor (Cys4)subfamily 1 (Thyroid hormone (α, β), CAR, FXR, LXR (α, β), PPAR (α, β/δ, γ), PXR, RAR (α, β, γ), ROR (α, β, γ), Rev-ErbA (α, β), VDR)
subfamily 2 (COUP-TF (I, II), Ear-2, HNF4 (α, γ), PNR, RXR (α, β, γ), Testicular receptor (2, 4), TLX)
subfamily 3 (Steroid hormone (Androgen, Estrogen (α, β), Glucocorticoid, Mineralocorticoid, Progesterone), Estrogen related (α, β, γ))
subfamily 4 NUR (NGFIB, NOR1, NURR1) · subfamily 5 (LRH-1, SF1) · subfamily 6 (GCNF) · subfamily 0 (DAX1, SHP)(2.2) Other Cys4(2.3) Cys2His2General transcription factors (TFIIA, TFIIB, TFIID, TFIIE (1, 2), TFIIF (1, 2), TFIIH (1, 2, 4, 2I, 3A, 3C1, 3C2))
ATBF1 · BCL (6, 11A, 11B) · CTCF · E4F1 · EGR (1, 2, 3, 4) · ERV3 · GFI1 · GLI-Krüppel family (1, 2, 3, REST, S2, YY1) · HIC (1, 2) · HIVEP (1, 2, 3) · IKZF (1, 2, 3) · ILF (2, 3) · KLF (2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 17) · MTF1 · MYT1 · OSR1 · PRDM9 · SALL (1, 2, 3, 4) · SP (1, 2, 4, 7, 8) · TSHZ3 · WT1 · Zbtb7 (7A, 7B) · ZBTB (16, 17, 20, 32, 33, 40) · zinc finger (3, 7, 9, 10, 19, 22, 24, 33B, 34, 35, 41, 43, 44, 51, 74, 143, 146, 148, 165, 202, 217, 219, 238, 239, 259, 267, 268, 281, 295, 300, 318, 330, 346, 350, 365, 366, 384, 423, 451, 452, 471, 593, 638, 644, 649, 655)(2.4) Cys6(2.5) Alternating composition(3) Helix-turn-helix domains (3.1) HomeodomainARX · CDX (1, 2) · CRX · CUTL1 · DBX (1, 2) · DLX (3, 4, 5) · EMX2 · EN (1, 2) · FHL (1, 2, 3) · HESX1 · HHEX · HLX · Homeobox (A1, A2, A3, A4, A5, A7, A9, A10, A11, A13, B1, B2, B3, B4, B5, B6, B7, B8, B9, B13, C4, C5, C6, C8, C9, C10, C11, C13, D1, D3, D4, D8, D9, D10, D11, D12, D13) · HOPX · IRX (1, 2, 3, 4, 5, 6, MKX) · LMX (1A, 1B) · MEIS (1, 2) · MEOX2 · MNX1 · MSX (1, 2) · NANOG · NKX (2-1, 2-2, 2-3, 2-5, 3-1, 3-2, 6-1, 6-2) · NOBOX · PBX (1, 2, 3) · PHF (1, 3, 6, 8, 10, 16, 17, 20, 21A) · PHOX (2A, 2B) · PITX (1, 2, 3) · POU domain (PIT-1, BRN-3: A, B, C, Octamer transcription factor: 1, 2, 3/4, 6, 7, 11) · OTX (1, 2) · PDX1 · SATB2 · SHOX2 · VAX1 · ZEB (1, 2)(3.2) Paired box(3.3) Fork head / winged helix(3.4) Heat Shock Factors(3.5) Tryptophan clusters(3.6) TEA domain(4) β-Scaffold factors with minor groove contacts (4.1) Rel homology region(4.2) STAT(4.3) p53(4.4) MADS box(4.6) TATA binding proteins(4.7) High-mobility group(4.10) Cold-shock domainCSDA, YBX1(4.11) Runt(0) Other transcription factors (0.2) HMGI(Y)(0.3) Pocket domain(0.6) Miscellaneoussee also transcription factor/coregulator deficiencies
B bsyn: dna (repl, cycl, reco, repr) · tscr (fact, tcrg, nucl, rnat, rept, ptts) · tltn (risu, pttl, nexn) · dnab, rnab/runp · stru (domn, 1°, 2°, 3°, 4°)Categories:- Human proteins
- Gene expression
- Chromosome 1 gene stubs
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