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Philos Trans R Soc Lond B Biol Sci. 2013 Sep 23;368(1629):20130005. doi: 10.1098/rstb.2013.0005. Print 2013.

Actin polymerization or myosin contraction: two ways to build up cortical tension for symmetry breaking.

Author information

1
Centre de Recherche, Institut Curie, , Paris 75248, France.

Abstract

Cells use complex biochemical pathways to drive shape changes for polarization and movement. One of these pathways is the self-assembly of actin filaments and myosin motors that together produce the forces and tensions that drive cell shape changes. Whereas the role of actin and myosin motors in cell polarization is clear, the exact mechanism of how the cortex, a thin shell of actin that is underneath the plasma membrane, can drive cell shape changes is still an open question. Here, we address this issue using biomimetic systems: the actin cortex is reconstituted on liposome membranes, in an 'outside geometry'. The actin shell is either grown from an activator of actin polymerization immobilized at the membrane by a biotin-streptavidin link, or built by simple adsorption of biotinylated actin filaments to the membrane, in the presence or absence of myosin motors. We show that tension in the actin network can be induced either by active actin polymerization on the membrane via the Arp2/3 complex or by myosin II filament pulling activity. Symmetry breaking and spontaneous polarization occur above a critical tension that opens up a crack in the actin shell. We show that this critical tension is reached by growing branched networks, nucleated by the Arp2/3 complex, in a concentration window of capping protein that limits actin filament growth and by a sufficient number of motors that pull on actin filaments. Our study provides the groundwork to understanding the physical mechanisms at work during polarization prior to cell shape modifications.

KEYWORDS:

acto-myosin; biomimetic liposome; cortical tension; symmetry breaking

PMID:
24062578
PMCID:
PMC3785958
DOI:
10.1098/rstb.2013.0005
[Indexed for MEDLINE]
Free PMC Article

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