Putting the brakes on a myosin motor

Casey Eddington; Margaret A. Titus

doi:10.1074/jbc.H120.013153

Putting the brakes on a myosin motor

Research output: Contribution to journal › Review article › peer-review

Abstract

Insulin-stimulated trafficking of GLUT4 requires the myosin motor Myo1C and signaling adaptor 14-3-3β. Originally, it was thought that 14-3-3β promotes GLUT4 transport by binding the Myo1C lever arm and activating the Myo1C motor. New work by Ji and Ostap using in vitro assays reveals that 14-3-3β binding actually inhibits Myo1C motility, prompting reconsideration of the functional relationship between 14-3-3β and Myo1C and the regulatory potential of atypical light chains.

Original language	English (US)
Pages (from-to)	3757-3758
Number of pages	2
Journal	Journal of Biological Chemistry
Volume	295
Issue number	12
DOIs	https://doi.org/10.1074/jbc.H120.013153
State	Published - Mar 20 2020

Bibliographical note

Funding Information:
This work is supported by National Institutes of Health Grants R01GM122917 and R01GM122917-01S1. The authors declare that they have no conflicts of interest with the contents of this article. The content is solely the respon-sibility of the authors and does not necessarily represent the official views of the National Institutes of Health.

Publisher Copyright:
© 2020 Eddington and Titus. Published under exclusive license by The American Society for Biochemistry and Molecular Biology, Inc.

PubMed: MeSH publication types

Journal Article
Research Support, N.I.H., Extramural
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abstract = "Insulin-stimulated trafficking of GLUT4 requires the myosin motor Myo1C and signaling adaptor 14-3-3β. Originally, it was thought that 14-3-3β promotes GLUT4 transport by binding the Myo1C lever arm and activating the Myo1C motor. New work by Ji and Ostap using in vitro assays reveals that 14-3-3β binding actually inhibits Myo1C motility, prompting reconsideration of the functional relationship between 14-3-3β and Myo1C and the regulatory potential of atypical light chains.",

author = "Casey Eddington and Titus, {Margaret A.}",

note = "Funding Information: This work is supported by National Institutes of Health Grants R01GM122917 and R01GM122917-01S1. The authors declare that they have no conflicts of interest with the contents of this article. The content is solely the respon-sibility of the authors and does not necessarily represent the official views of the National Institutes of Health. Publisher Copyright: {\textcopyright} 2020 Eddington and Titus. Published under exclusive license by The American Society for Biochemistry and Molecular Biology, Inc.",

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AU - Titus, Margaret A.

N1 - Funding Information: This work is supported by National Institutes of Health Grants R01GM122917 and R01GM122917-01S1. The authors declare that they have no conflicts of interest with the contents of this article. The content is solely the respon-sibility of the authors and does not necessarily represent the official views of the National Institutes of Health. Publisher Copyright: © 2020 Eddington and Titus. Published under exclusive license by The American Society for Biochemistry and Molecular Biology, Inc.

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N2 - Insulin-stimulated trafficking of GLUT4 requires the myosin motor Myo1C and signaling adaptor 14-3-3β. Originally, it was thought that 14-3-3β promotes GLUT4 transport by binding the Myo1C lever arm and activating the Myo1C motor. New work by Ji and Ostap using in vitro assays reveals that 14-3-3β binding actually inhibits Myo1C motility, prompting reconsideration of the functional relationship between 14-3-3β and Myo1C and the regulatory potential of atypical light chains.

AB - Insulin-stimulated trafficking of GLUT4 requires the myosin motor Myo1C and signaling adaptor 14-3-3β. Originally, it was thought that 14-3-3β promotes GLUT4 transport by binding the Myo1C lever arm and activating the Myo1C motor. New work by Ji and Ostap using in vitro assays reveals that 14-3-3β binding actually inhibits Myo1C motility, prompting reconsideration of the functional relationship between 14-3-3β and Myo1C and the regulatory potential of atypical light chains.

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Putting the brakes on a myosin motor

Abstract

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