Miogenina

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Miogenina (factor miogénico 4)
Identificadores
Símbolos MYOG; MYF4; bHLHc3; myf-4
ID externos OMIM: 159980 MGI97276 HomoloGene1854 GeneCards: MYOG Gene
Padrões de expressão do ARN
PBB GE MYOG 207282 s at tn.png
Mais dados de expressão
Ortólogos
Espécies Humano Rato
Entrez 4656 17928
Ensembl ENSG00000122180 ENSMUSG00000026459
UniProt P15173 P12979
RefSeq (mRNA) NM_002479.5 NM_031189.2
RefSeq (proteína) NP_002470.2 NP_112466.1
Localização (UCSC) Chr 1:
203.05 – 203.06 Mb
Chr 1:
134.29 – 134.29 Mb
Busca PubMed [1] [2]

A miogenina (factor miogénico 4), também conhecido como MYOG, é um gene.[1]

A miogenina é um factor de transcrição em hélice-volta-hélice básico, específico dos músculos, que está envolvido na coordenação do desenvolvimento e reparação do músculo esquelético. A miogenina é um membro da família de factores de transcrição MyoD, que também incluí MyoD, Myf5 e Mrf4.

No rato, a miogenina é essencial para o desenvolvimento de músculo esquelético funcional. Quando o ADN que codifica a miogenina é desactivado do genoma do rato, são observados severos defeitos dos músculos esqueléticos. Ratos que carecem de ambas as cópias de miogenina sofrem deletalidade perinatal devido à falta de fibras maduras secundárias de músculo esquelético por todo o corpo.

Em cultura celular, a miogenina pode induzir a miogénese numa variedade de tipos celulares não musculares.

Interacções[editar | editar código-fonte]

Observou-se a interacção da miogenina com POLR2C,[2] Factor de transcrição Sp1,[3] TCF3,[4] [5] Factor de resposta ao soro[3] [6] e MDFI.[7]

Referências

  1. Entrez Gene: MYOG myogenin (myogenic factor 4).
  2. 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. 16 (12): 1639–41. DOI:10.1096/fj.02-0123fje. PMID 12207009.
  3. 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. 19 (4): 2577–84. ISSN 0270-7306. PMID 10082523.
  4. 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. 272 (32): 19785–93. DOI:10.1074/jbc.272.32.19785. ISSN 0021-9258. PMID 9242638.
  5. 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. 267 (25): 17498–501. ISSN 0021-9258. PMID 1325437.
  6. 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. 271 (9): 5258–64. DOI:10.1074/jbc.271.9.5258. ISSN 0021-9258. PMID 8617811.
  7. 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 86 (5): 731–41. DOI:10.1016/S0092-8674(00)80148-8. ISSN 0092-8674. PMID 8797820.

Leitura adicional[editar | editar código-fonte]

  • 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. PMID 1329097.
  • 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. 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. PMID 1850513.
  • 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. PMID 2583111.
  • 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. 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. PMID 10082523.
  • 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. 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, 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. PMID 12477932.

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