Reconstituting the actin cytoskeleton at or near surfaces in vitro

Biochim Biophys Acta. 2015 Nov;1853(11 Pt B):3006-14. doi: 10.1016/j.bbamcr.2015.07.021. Epub 2015 Jul 31.

Abstract

Actin filament dynamics have been studied for decades in pure protein solutions or in cell extracts, but a breakthrough in the field occurred at the turn of the century when it became possible to reconstitute networks of actin filaments, growing in a controlled but physiological manner on surfaces, mimicking the actin assembly that occurs at the plasma membrane during cell protrusion and cell shape changes. The story begins with the bacteria Listeria monocytogenes, the study of which led to the reconstitution of cellular actin polymerization on a variety of supports including plastic beads. These studies made possible the development of liposome-type substrates for filament assembly and micropatterning of actin polymerization nucleation. Based on the accumulated expertise of the last 15 years, many exciting approaches are being developed, including the addition of myosin to biomimetic actin networks to study the interplay between actin structure and contractility. The field is now poised to make artificial cells with a physiological and dynamic actin cytoskeleton, and subsequently to put these cells together to make in vitro tissues. This article is part of a Special Issue entitled: Mechanobiology.

Keywords: Actin cortex; Actin polymerization; Actin-based motility; Biomimetic systems; Contractility; Lamellipodium.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Actin Cytoskeleton / chemistry*
  • Actin Cytoskeleton / metabolism
  • Animals
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / metabolism
  • Humans
  • Listeria monocytogenes / chemistry*
  • Listeria monocytogenes / metabolism
  • Membrane Proteins / chemistry*
  • Membrane Proteins / metabolism

Substances

  • Bacterial Proteins
  • Membrane Proteins