Miogenina
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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 inclui 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
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
- ↑ «Entrez Gene: MYOG myogenin (myogenic factor 4)»
- ↑ Corbi, Nicoletta; Di Padova Monica, De Angelis Roberta, Bruno Tiziana, Libri Valentina, Iezzi Simona, Floridi Aristide, Fanciulli Maurizio, Passananti Claudio (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». United States. FASEB J. 16 (12): 1639–41. PMID 12207009. doi:10.1096/fj.02-0123fje
- ↑ a b 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». UNITED STATES. Mol. Cell. Biol. 19 (4): 2577–84. ISSN 0270-7306. PMC 84050
. PMID 10082523
- ↑ Langlands, K; Yin X, Anand G, Prochownik E V (1997). «Differential interactions of Id proteins with basic-helix-loop-helix transcription factors». UNITED STATES. J. Biol. Chem. 272 (32): 19785–93. ISSN 0021-9258. PMID 9242638. doi:10.1074/jbc.272.32.19785
- ↑ Chakraborty, T; Martin J F, Olson E N (1992). «Analysis of the oligomerization of myogenin and E2A products in vivo using a two-hybrid assay system». UNITED STATES. J. Biol. Chem. 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 (1996). «Physical interaction between the mitogen-responsive serum response factor and myogenic basic-helix-loop-helix proteins». UNITED STATES. J. Biol. Chem. 271 (9): 5258–64. ISSN 0021-9258. PMID 8617811. doi:10.1074/jbc.271.9.5258
- ↑ Chen, C M; Kraut N, Groudine M, Weintraub H (1996). «I-mf, a novel myogenic repressor, interacts with members of the MyoD family». UNITED STATES. Cell. 86 (5): 731–41. ISSN 0092-8674. PMID 8797820. doi:10.1016/S0092-8674(00)80148-8
Leitura adicional editar
- 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. PMID 1846704. doi:10.1126/science.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. PMC 50156 . PMID 1329097. doi:10.1073/pnas.89.20.9484
- 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. PMID 1649701. doi:10.1016/0092-8674(91)90620-E
- 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. PMC 2289955 . PMID 1659574. doi:10.1083/jcb.115.4.905
- Pearson-White SH (1991). «Human MyoD: cDNA and deduced amino acid sequence.». Nucleic Acids Res. 19 (5). 1148 páginas. PMC 333794 . PMID 1850513. doi:10.1093/nar/19.5.1148
- 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. PMID 1962752. doi:10.1016/0888-7543(90)90028-S
- 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. PMID 2163343. doi:10.1101/gad.4.4.582
- 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
- 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. PMID 8617811. doi:10.1074/jbc.271.9.5258
- 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. PMID 8797820. doi:10.1016/S0092-8674(00)80148-8
- 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
- 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. PMID 9242638. doi:10.1074/jbc.272.32.19785
- 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
- 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. PMID 10329008. doi:10.1006/geno.1998.5719
- 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. PMC 148632 . PMID 10471746. doi:10.1093/nar/27.18.3752
- 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. PMID 10757985. doi:10.1021/bi992533u
- 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. PMID 12207009. doi:10.1096/fj.02-0123fje
- 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. PMC 139241 . PMID 12477932. doi:10.1073/pnas.242603899
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