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

doi:10.1074/jbc.M113.511014

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

Department of Cell and Biological Systems

Research output: Contribution to journal › Article › peer-review

28 Scopus citations

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 language	English (US)
Pages (from-to)	37126-37137
Number of pages	12
Journal	Journal of Biological Chemistry
Volume	288
Issue number	52
DOIs	https://doi.org/10.1074/jbc.M113.511014
State	Published - Dec 27 2013

All Science Journal Classification (ASJC) codes

Biochemistry
Molecular Biology
Cell Biology

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10.1074/jbc.M113.511014

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title = "Myosin 3A kinase activity is regulated by phosphorylation of the kinase domain activation loop",

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.",

author = "Quintero, \{Omar A.\} and Unrath, \{William C.\} and Stevens, \{Stanley M.\} and Uri Manor and Bechara Kachar and Yengo, \{Christopher M.\}",

year = "2013",

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doi = "10.1074/jbc.M113.511014",

language = "English (US)",

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T1 - Myosin 3A kinase activity is regulated by phosphorylation of the kinase domain activation loop

AU - Quintero, Omar A.

AU - Unrath, William C.

AU - Stevens, Stanley M.

AU - Manor, Uri

AU - Kachar, Bechara

AU - Yengo, Christopher M.

PY - 2013/12/27

Y1 - 2013/12/27

N2 - 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.

AB - 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.

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AN - SCOPUS:84891381020

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SP - 37126

EP - 37137

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

IS - 52

ER -

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

Abstract

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