Mirk/dyrk1B decreases the nuclear accumulation of class II histone deacetylases during skeletal muscle differentiation - PubMed (original) (raw)
. 2005 Feb 11;280(6):4894-905.
doi: 10.1074/jbc.M411894200. Epub 2004 Nov 16.
Affiliations
- PMID: 15546868
- DOI: 10.1074/jbc.M411894200
Free article
Mirk/dyrk1B decreases the nuclear accumulation of class II histone deacetylases during skeletal muscle differentiation
Xiaobing Deng et al. J Biol Chem. 2005.
Free article
Abstract
Mirk/dyrk1B is a member of the dyrk/minibrain family of serine/threonine kinases that mediate the transition from growth to differentiation in lower eukaryotes and mammals. Depletion of endogenous Mirk from C2C12 myoblasts by RNA interference blocks skeletal muscle differentiation (Deng, X., Ewton, D., Pawlikowski, B., Maimone, M., and Friedman, E. (2003) J. Biol. Chem. 278, 41347-41354). We now demonstrate that knockdown of Mirk blocks transcription of the muscle regulatory factor myogenin. Co-expression of Mirk with MEF2C, but not MyoD or Myf5, enhanced activation of the myogenin promoter in a Mirk kinase-dependent manner. Mirk activated MEF2 not through direct phosphorylation of MEF2 but by phosphorylation of its inhibitors, the class II histone deacetylases (HDACs). MEF2 is sequestered by class II HDACs such as HDAC5 and MEF2-interacting transcriptional repressor (MITR). Mirk antagonized the inhibition of MEF2C by MITR, whereas kinase-inactive Mirk was ineffective. Mirk phosphorylates class II HDACs at a conserved site within the nuclear localization region, reducing their nuclear accumulation in a dose-dependent and kinase-dependent manner. Moreover, less mutant MITR phosphomimetic at the Mirk phosphorylation site localized in the nucleus than wild-type MITR. Regulation of class II HDACs occurs by multiple mechanisms. Others have shown that calcium signaling leads to phosphorylation of HDACs at 14-3-3-binding sites, blocking their association with MEF2 within the nucleus. Mirk provides another level of regulation. Mirk is induced within the initial 24 h of myogenic differentiation and enables MEF2 to transcribe the myogenin gene by decreasing the nuclear accumulation of class II HDACs.
Similar articles
- Mirk/dyrk1B is a Rho-induced kinase active in skeletal muscle differentiation.
Deng X, Ewton DZ, Pawlikowski B, Maimone M, Friedman E. Deng X, et al. J Biol Chem. 2003 Oct 17;278(42):41347-54. doi: 10.1074/jbc.M306780200. Epub 2003 Aug 5. J Biol Chem. 2003. PMID: 12902328 - The cyclin-dependent kinase inhibitor p27Kip1 is stabilized in G(0) by Mirk/dyrk1B kinase.
Deng X, Mercer SE, Shah S, Ewton DZ, Friedman E. Deng X, et al. J Biol Chem. 2004 May 21;279(21):22498-504. doi: 10.1074/jbc.M400479200. Epub 2004 Mar 9. J Biol Chem. 2004. PMID: 15010468 - Association of class II histone deacetylases with heterochromatin protein 1: potential role for histone methylation in control of muscle differentiation.
Zhang CL, McKinsey TA, Olson EN. Zhang CL, et al. Mol Cell Biol. 2002 Oct;22(20):7302-12. doi: 10.1128/MCB.22.20.7302-7312.2002. Mol Cell Biol. 2002. PMID: 12242305 Free PMC article. - Synergistic up-regulation of muscle LIM protein expression in C2C12 and NIH3T3 cells by myogenin and MEF2C.
Ji ZX, Du C, Wu GS, Li SY, An GS, Yang YX, Jia R, Jia HT, Ni JH. Ji ZX, et al. Mol Genet Genomics. 2009 Jan;281(1):1-10. doi: 10.1007/s00438-008-0393-7. Epub 2008 Nov 6. Mol Genet Genomics. 2009. PMID: 18987887 Review. - Regulation and functions of myogenic regulatory factors in lower vertebrates.
Rescan PY. Rescan PY. Comp Biochem Physiol B Biochem Mol Biol. 2001 Aug;130(1):1-12. doi: 10.1016/s1096-4959(01)00412-2. Comp Biochem Physiol B Biochem Mol Biol. 2001. PMID: 11470439 Review.
Cited by
- New insights into the roles for DYRK family in mammalian development and congenital diseases.
Yoshida S, Yoshida K. Yoshida S, et al. Genes Dis. 2022 Jan 6;10(3):758-770. doi: 10.1016/j.gendis.2021.12.004. eCollection 2023 May. Genes Dis. 2022. PMID: 37396550 Free PMC article. Review. - Structures of Down syndrome kinases, DYRKs, reveal mechanisms of kinase activation and substrate recognition.
Soundararajan M, Roos AK, Savitsky P, Filippakopoulos P, Kettenbach AN, Olsen JV, Gerber SA, Eswaran J, Knapp S, Elkins JM. Soundararajan M, et al. Structure. 2013 Jun 4;21(6):986-96. doi: 10.1016/j.str.2013.03.012. Epub 2013 May 9. Structure. 2013. PMID: 23665168 Free PMC article. - Direct interaction between myocyte enhancer factor 2 (MEF2) and protein phosphatase 1alpha represses MEF2-dependent gene expression.
Perry RL, Yang C, Soora N, Salma J, Marback M, Naghibi L, Ilyas H, Chan J, Gordon JW, McDermott JC. Perry RL, et al. Mol Cell Biol. 2009 Jun;29(12):3355-66. doi: 10.1128/MCB.00227-08. Epub 2009 Apr 13. Mol Cell Biol. 2009. PMID: 19364819 Free PMC article. - Mirk regulates the exit of colon cancer cells from quiescence.
Jin K, Ewton DZ, Park S, Hu J, Friedman E. Jin K, et al. J Biol Chem. 2009 Aug 21;284(34):22916-25. doi: 10.1074/jbc.M109.035519. Epub 2009 Jun 19. J Biol Chem. 2009. PMID: 19542220 Free PMC article. - The myogenic kinome: protein kinases critical to mammalian skeletal myogenesis.
Knight JD, Kothary R. Knight JD, et al. Skelet Muscle. 2011 Sep 8;1:29. doi: 10.1186/2044-5040-1-29. Skelet Muscle. 2011. PMID: 21902831 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Molecular Biology Databases