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 journalArticle

13 Citations (Scopus)

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

Fingerprint

Myosin-Light-Chain Kinase
Phosphorylation
Myosins
Phosphotransferases
Chemical activation
Myosin Type III
Actins
Motor Activity
Epithelium
Maintenance

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Quintero, Omar A. ; Unrath, William C. ; Stevens, Stanley M. ; Manor, Uri ; Kachar, Bechara ; Yengo, Christopher M. / Myosin 3A kinase activity is regulated by phosphorylation of the kinase domain activation loop. In: Journal of Biological Chemistry. 2013 ; Vol. 288, No. 52. pp. 37126-37137.
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Myosin 3A kinase activity is regulated by phosphorylation of the kinase domain activation loop. / Quintero, Omar A.; Unrath, William C.; Stevens, Stanley M.; Manor, Uri; Kachar, Bechara; Yengo, Christopher M.

In: Journal of Biological Chemistry, Vol. 288, No. 52, 27.12.2013, p. 37126-37137.

Research output: Contribution to journalArticle

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AU - Yengo, Christopher M.

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