4.5 Article

Force-history dependence and cyclic mechanical reinforcement of actin filaments at the single molecular level

Journal

JOURNAL OF CELL SCIENCE
Volume 132, Issue 4, Pages -

Publisher

COMPANY BIOLOGISTS LTD
DOI: 10.1242/jcs.216911

Keywords

Actin; Mechanotransduction; Atomic force microscopy (AFM); Single-molecule biophysics

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Funding

  1. National Institutes of Health [R01 HL18671, U01 CA214354, R01 AR048615]

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The actin cytoskeleton is subjected to dynamic mechanical forces over time and the history of force loading may serve as mechanical preconditioning. While the actin cytoskeleton is known to be mechanosensitive, the mechanisms underlying force regulation of actin dynamics still need to be elucidated. Here, we investigated actin depolymerization under a range of dynamic tensile forces using atomic force microscopy. Mechanical loading by cyclic tensile forces induced significantly enhanced bond lifetimes and different force-loading histories resulted in different dissociation kinetics in G-actin-G-actin and G-actin-F-actin interactions. Actin subunits at the two ends of filaments formed bonds with distinct kinetics under dynamic force, with cyclic mechanical reinforcement more effective at the pointed end compared to that at the barbed end. Our data demonstrate force-history dependent reinforcement in actin-actin bonds and polarity of the actin depolymerization kinetics under cyclic tensile forces. These properties of actin may be important clues to understanding regulatory mechanisms underlying actin-dependent mechanotransduction and mechanosensitive cytoskeletal dynamics.

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