Passer à la navigation principale Passer à la recherche Passer au contenu principal

Biomimetic systems shed light on actin-based motility down to the molecular scale

  • Guillaume Romet-Lemonne
  • , Emmanuel Helfer
  • , Vincent Delatour
  • , Beata Bugyi
  • , Montserrat Bosch
  • , Stephane Romero
  • , Marie France Carleir
  • , Stephan Schmidt
  • , Andreas Fery
  • CNRS-UPR U. Propre de Recherche 9063
  • Laboratoire National de Métrologie et d'Essais
  • CNRS UMR 5237
  • Collège de France
  • Department of Physical Chemistry II
  • University of Bayreuth

Résultats de recherche: Contribution à un journal › Article › Revue par des pairs

1 Citation (Scopus)

Résumé

Cell motility, one of the modular activities of living cells, elicits the response of the cell to extra-cellular signals, to move directionally, feed, divide or transport materials. The combined actions of molecular motors and re-modeling of the cytoskeleton generate forces and movement. Here we describe mechanistic approaches of force and movement produced by site-directed assembly of actin filaments. The insight derived from a biochemical analysis of the protein machineries involved in "actin-based motile processes" like cell protrusions, invaginations, organelle propulsion, is used to build reconstituted assays that mimic cellular processes, using several protein machineries known to initiate filament assembly by different mechanisms. Reconstitution of complex self-organized systems presents a broad variety of interests. Reconstituting actin-based movement of a functionalized particle from a minimum number of pure proteins, first used to prove the general thermodynamic principles at work in motility, then was the basis for fully controlled physical measurements of forces produced by polymerization of actin against an obstacle and of the mechanical properties of the resulting polymer arrays. In addition, measurements at the mesoscopic scale (trajectories, velocity, polymer mechanics, fluorescence of specifically labeled components of the actin array, use of mutated proteins) can provide further insight into the molecular mechanisms underlying motility.

langue originaleAnglais
Pages (de - à)5-15
Nombre de pages11
journalBiophysical Reviews and Letters
Volume4
Numéro de publication1-2
Les DOIs
étatPublié - 1 janv. 2009
Modification externeOui

Empreinte digitale

Examiner les sujets de recherche de « Biomimetic systems shed light on actin-based motility down to the molecular scale ». Ensemble, ils forment une empreinte digitale unique.

Contient cette citation