Aurora kinase A-mediated phosphorylation of mPOU at a specific site drives skeletal muscle differentiation

Dhanasekan Karthigeyan, Arnab Bose, Ramachandran Boopathi, Vinay Jaya Rao, Hiroki Shima, Narendra Bharathy, Kazuhiko Igarashi, Reshma Taneja, Arun Kumar Trivedi, Tapas K. Kundu

Research output: Contribution to journalArticlepeer-review

Abstract

Aurora kinases are Ser/Thr-directed protein kinases which play pivotal roles in mitosis. Recent evidences highlight 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.

Original languageEnglish
Pages (from-to)195-201
Number of pages7
JournalJournal of biochemistry
Volume167
Issue number2
DOIs
Publication statusPublished - 2020 Feb 1

Keywords

  • Aurora kinase A
  • DNA binding
  • mPOU
  • mitosis
  • skeletal muscle differentiation

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

Fingerprint Dive into the research topics of 'Aurora kinase A-mediated phosphorylation of mPOU at a specific site drives skeletal muscle differentiation'. Together they form a unique fingerprint.

Cite this