title: Mechanotransduction down to individual actin filaments.
abstract: The actin cytoskeleton plays an essential role in a cell's ability to generate and sense forces, both internally and in interaction with the outside world. The transduction of mechanical cues into biochemical reactions in cells, in particular, is a multi-scale process which requires a variety of approaches to be understood. This review focuses on understanding how mechanical stress applied to an actin filament can affect its assembly dynamics. Today, experiments addressing this issue at the scale of individual actin filaments are emerging and bring novel insight into mechanotransduction. For instance, recent data show that actin filaments can act as mechanosensors, as an applied tension or curvature alters their conformation and their affinity for regulatory proteins. Filaments can also transmit mechanical tension to other proteins, which consequently change the way they interact with the filaments to regulate their assembly. These results provide evidence for mechanotransduction at the scale of individual filaments, showing that forces participate in the regulation of filament assembly and organization. They bring insight into the elementary events coupling mechanics and biochemistry in cells. The experiments presented here are linked to recent technical developments, and certainly announce the advent of more exciting results in the future.
authors.affiliation: Laboratoire d'Enzymologie et Biochimie Structurales, CNRS, 91190 Gif-sur-Yvette, France. Electronic address: romet@lebs.cnrs-gif.fr.
authors.forename: Guillaume
authors.initials: G
authors.lastname: Romet-Lemonne
authors.forename: Antoine
authors.initials: A
authors.lastname: Jégou
mesh_terms: D008841:Actin Cytoskeleton / Q000378:metabolism*; D000199:Actins / Q000378:metabolism*; D000818:Animals; D006801:Humans; D040542:Mechanotransduction, Cellular / Q000502:physiology*; D013314:Stress, Mechanical
chemical_list: D000199:Actins
keywords: ADF; ADP; AFM; ATP; Actin dynamics; Cell mechanics; Cryo-EM; F-actin; Forces; Formin; G-actin; Mechanosensitivity; Microfluidics; Optical traps; Regulatory proteins; Single filament; TIRF; Tension; actin depolymerizing factor; adenosine diphosphate; adenosine triphosphate; atomic force microscopy; cryoelectron microscopy; filamentous actin; globular (monomeric) actin; mDia1; mammalian diaphanous 1; total internal reflection fluorescence