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Myosin 3A kinase activity is regulated by phosphorylation of the kinase domain activation loop

  • Omar A. Quintero
  • , William C. Unrath
  • , Stanley M. Stevens
  • , Uri Manor
  • , Bechara Kachar
  • , Christopher M. Yengo

Research output: Contribution to journalArticlepeer-review

Abstract

Background: Class III myosins contain both a motor and kinase domain. Results: Phosphorylation of the kinase activation loop enhances MYO3A kinase activity, augmenting autophosphorylation induced attenuation of motor and cellular activity. Conclusion: MYO3A kinase activity mediates localization and function within actin protrusions. Significance: Characterizing MYO3A kinase regulation enhances our understanding of the role of MYO3A in the maintenance of actin protrusions found in sensory epithelia.

Original languageEnglish (US)
Pages (from-to)37126-37137
Number of pages12
JournalJournal of Biological Chemistry
Volume288
Issue number52
DOIs
StatePublished - Dec 27 2013

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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