Myosin-dependent actin stabilization as revealed by single-molecule imaging of actin turnover

Molecular Biology of the Cell
Sawako YamashiroNaoki Watanabe

Abstract

How mechanical stress applied to the actin network modifies actin turnover has attracted considerable attention. Actomyosin exerts the major force on the actin network, which has been implicated in actin stability regulation. However, direct monitoring of immediate changes in F-actin stability on alteration of actomyosin contraction has not been achieved. Here we reexamine myosin regulation of actin stability by using single-molecule speckle analysis of actin. To avoid possible errors attributable to actin-binding probes, we employed DyLight-labeled actin that distributes identical to F-actin in lamellipodia. We performed time-resolved analysis of the effect of blebbistatin on actin turnover. Blebbistatin enhanced actin disassembly in lamellipodia of fish keratocytes and lamellar of Xenopus XTC cells at an early stage of the inhibition, indicating that actomyosin contraction stabilizes cellular F-actin. In addition, our data show a previously unrecognized relationship between the actin network-driving force and the actin turnover rates in lamellipodia. These findings point to the power of direct viewing of molecular behavior in elucidating force regulation of actin filament turnover.

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Citations

Jul 18, 2019·Journal of Muscle Research and Cell Motility·Sawako Yamashiro, Naoki Watanabe
May 23, 2020·Science Advances·Steven J TanAlexander R Dunn
Sep 26, 2019·Molecular Biology of the Cell·Anna B KobbRodrigo Fernandez-Gonzalez
Jan 24, 2021·Proceedings of the National Academy of Sciences of the United States of America·Christoph SchreiberMartin Falcke
Dec 19, 2018·Biophysical Journal·Sawako YamashiroNaoki Watanabe

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Methods Mentioned

BETA
fluorescence recovery after photobleaching

Software Mentioned

Lifeact
qFSM
SiMS
Speckle TrackerJ

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