Journal
JOURNAL OF BIOCHEMISTRY
Volume 167, Issue 2, Pages 195-201Publisher
OXFORD UNIV PRESS
DOI: 10.1093/jb/mvz088
Keywords
Aurora kinase A; DNA binding; mitosis; mPOU; skeletal muscle differentiation
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Funding
- Department of Biotechnology, GOI, through Chromatin and Disease: Program Support [BT/01/CEIB/10/111/01]
- Indo-Japan bilateral joint research program by Department of Science and Technology, India
- Japan Society for the Promotion of Science (JSPS), Japan
- JSPS [17K07278, 25670156]
- Grants-in-Aid for Scientific Research [17K07278, 25670156] Funding Source: KAKEN
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Aurora kinases are Ser/Thr-directed protein kinases which play pivotal roles in mitosis. Recent evidences high-light the importance of these kinases in multiple biological events including skeletal muscle differentiation. Our earlier study identified the transcription factor POU6F1 (or mPOU) as a novel Aurora kinase (Aurk) A substrate. Here, we report that Aurora kinase A phosphorylates mPOU at Ser197 and inhibit its DNA-binding ability. Delving into mPOU physiology, we find that the phospho-mimic (S197D) mPOU mutant exhibits enhancement, while the wild type or the phospho-deficient mutant shows retardation in C2C12 myoblast differentiation. Interestingly, POU6F1 depletion phenocopies S197D-mPOU overexpression in the differentiation context. Collectively, our results signify mPOU as a negative regulator of skeletal muscle differentiation and strengthen the importance of AurkA in skeletal myogenesis.
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