title: Actin-based motility: from molecules to movement.
abstract: Extensive progress has been made recently in understanding the mechanism by which cells move and extend protrusions using site-directed polymerization of actin in response to signalling. Insights into the molecular mechanism of production of force and movement by actin polymerization have been provided by a crosstalk between several disciplines, including biochemistry, biomimetic approaches and computational studies. This review focuses on the biochemical properties of the proteins involved in actin-based motility and shows how these properties are used to generate models of force production, how the predictions of different theoretical models are tested using a biochemically controlled reconstituted motility assay and how the changes in motility resulting from changes to the concentrations of components of the assay can help understand diverse aspects of the motile behavior of living cells.
authors.affiliation: Dynamique du Cytosquelette, LEBS, CNRS, 91198 Gif-sur-Yvette, France. carlier@lebs.cnrs-gif.fr
authors.forename: Marie-France
authors.initials: MF
authors.lastname: Carlier
authors.forename: Christophe
authors.initials: C
authors.lastname: Le Clainche
authors.forename: Sebastian
authors.initials: S
authors.lastname: Wiesner
authors.forename: Dominique
authors.initials: D
authors.lastname: Pantaloni
mesh_terms: D051377:Actin-Related Protein 2; D051378:Actin-Related Protein 3; D000199:Actins / Q000378:metabolism* / Q000648:ultrastructure; D000818:Animals; D002465:Cell Movement / Q000502:physiology*; D003598:Cytoskeletal Proteins / Q000378:metabolism*; D008954:Models, Biological; D009419:Nerve Tissue Proteins / Q000378:metabolism; D015398:Signal Transduction / Q000502:physiology*; D051317:Wiskott-Aldrich Syndrome Protein, Neuronal
chemical_list: D051377:Actin-Related Protein 2; D051378:Actin-Related Protein 3; D000199:Actins; D003598:Cytoskeletal Proteins; D009419:Nerve Tissue Proteins; D051317:Wiskott-Aldrich Syndrome Protein, Neuronal