UMMS Affiliation

Division of Cell Biology and Imaging, Department of Radiology

Publication Date

2019-09-02

Document Type

Article

Disciplines

Amino Acids, Peptides, and Proteins | Biochemistry | Cell Biology | Cells | Cellular and Molecular Physiology | Enzymes and Coenzymes | Molecular Biology | Structural Biology

Abstract

Myosin II is a motor protein with two heads and an extended tail that plays an essential role in cell motility. Its active form is a polymer (myosin filament) that pulls on actin to generate motion. Its inactive form is a monomer with a compact structure (10S sedimentation coefficient), in which the tail is folded and the two heads interact with each other, inhibiting activity. This conformation is thought to function in cells as an energy-conserving form of the molecule suitable for storage as well as transport to sites of filament assembly. The mechanism of inhibition of the compact molecule is not fully understood. We have performed a 3-D reconstruction of negatively stained 10S myosin from smooth muscle in the inhibited state using single-particle analysis. The reconstruction reveals multiple interactions between the tail and the two heads that appear to trap ATP hydrolysis products, block actin binding, hinder head phosphorylation, and prevent filament formation. Blocking these essential features of myosin function could explain the high degree of inhibition of the folded form of myosin thought to underlie its energy-conserving function in cells. The reconstruction also suggests a mechanism for unfolding when myosin is activated by phosphorylation.

Keywords

Myosin II, motor proteins, physiology

Rights and Permissions

© 2019 Yang et al. This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms/). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 International license, as described at https://creativecommons.org/licenses/by-nc-sa/4.0/).

DOI of Published Version

10.1085/jgp.201912431

Source

J Gen Physiol. 2019 Sep 2;151(9):1081-1093. doi: 10.1085/jgp.201912431. Epub 2019 Aug 6. Link to article on publisher's site

Journal/Book/Conference Title

The Journal of general physiology

Related Resources

Link to Article in PubMed

PubMed ID

31387899

Creative Commons License

Creative Commons Attribution-Noncommercial 4.0 License
This work is licensed under a Creative Commons Attribution-Noncommercial-Share Alike 4.0 License.

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