Reconstitution of an actin cortex inside a liposome.
The composite and versatile structure of the cytoskeleton confers complex mechanical properties on cells. Actin filaments sustain the cell membrane and their dynamics insure cell shape changes. For example, the lamellipodium moves by actin polymerization, a mechanism that has been studied using simplified experimental systems. Much less is known about the actin cortex, a shell-like structure underneath the membrane that contracts for cell movement. We have designed an experimental system that mimicks the cell cortex by allowing actin polymerization to nucleate and assemble at the inner membrane of a liposome. Actin shell growth can be triggered inside the liposome, which offers a useful system for a controlled study. The observed actin shell thickness and estimated mesh size of the actin structure are in good agreement with cellular data. Such a system paves the way for a thorough characterization of cortical dynamics and mechanics.
Pontani
Léa-Laetitia
LL
Laboratoire Physicochimie Curie, CNRS/Institut Curie/Université Paris, Paris, France.
van der Gucht
Jasper
J
Salbreux
Guillaume
G
Heuvingh
Julien
J
Joanny
Jean-François
JF
Sykes
Cécile
C
D008841:Actin Cytoskeleton / Q000737:chemistry*; D051376:Actin-Related Protein 2-3 Complex / Q000737:chemistry; D000199:Actins / Q000737:chemistry*; D000465:Algorithms; D002784:Cholesterol / Q000737:chemistry; D004655:Emulsions / Q000737:chemistry; D005453:Fluorescence; D008051:Lipid Bilayers / Q000737:chemistry; D008081:Liposomes / Q000737:chemistry*; D008956:Models, Chemical
D051376:Actin-Related Protein 2-3 Complex; D000199:Actins; D004655:Emulsions; D008051:Lipid Bilayers; D008081:Liposomes; D002784:Cholesterol