The central role of the tail in switching off 10S myosin II activity.

The Journal of General Physiology
Shixin YangR Craig

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 act...Continue Reading

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Citations

Aug 10, 2019·The Journal of General Physiology·Ben Short
Jun 24, 2020·Proceedings of the National Academy of Sciences of the United States of America·Xiong LiuEdward D Korn
Dec 18, 2019·Archives of Biochemistry and Biophysics·John L Woodhead, Roger Craig
Dec 4, 2020·Nature·Shixin YangRoger Craig
Dec 4, 2020·Nature·Charlotte A ScarffMichelle Peckham
Feb 20, 2021·The Journal of General Physiology·Lu WangChun Y Seow
Jul 28, 2021·Annual Review of Cell and Developmental Biology·Marina Garrido-CasadoMiguel Vicente-Manzanares
Dec 11, 2021·The Journal of General Physiology·Roger Craig, Raúl Padrón

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Datasets Mentioned

BETA
EMD-20084

Methods Mentioned

BETA
cross-linking study
cross-linking studies

Software Mentioned

JWEB
EMAN
RELION
UCSF Chimera
SPIDER

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