Dendritic branching and homogenization of actin networks mediated by arp2/3 complex.
The cytoskeleton of motile cells exploits accessory proteins to locally modulate its organization and micromechanics. Here, we demonstrate that the Arp2/3 complex plays the role, unique among other cytoskeleton proteins, of an actin network "homogenizer," promoting the extremely rapid formation of homogeneous and stiff networks. Nanotracking of microspheres imbedded in F-actin networks reveals that the Arp2/3 complex promotes the formation of networks that are remarkably more homogeneous than control networks, a distinctive feature that coordinates a dramatic burst of elasticity. These results suggest that the Arp2/3 complex possesses a unique function of stabilizing membrane protrusions through the formation of homogeneous and stiff actin cytoskeleton at the leading edge of crawling cells.
Tseng
Yiider
Y
Department of Chemical and Biomolecular Engineering, The Johns Hopkins University, 3400 N. Charles Street, Baltimore, Maryland 21218, USA.
Wirtz
Denis
D
D008841:Actin Cytoskeleton / Q000737:chemistry*; D051377:Actin-Related Protein 2; D051378:Actin-Related Protein 3; D000199:Actins / Q000138:chemical synthesis / Q000737:chemistry*; D003460:Crystallization / Q000379:methods*; D003598:Cytoskeletal Proteins / Q000737:chemistry*; D003599:Cytoskeleton / Q000737:chemistry; D020409:Molecular Motor Proteins / Q000138:chemical synthesis / Q000737:chemistry*
D051377:Actin-Related Protein 2; D051378:Actin-Related Protein 3; D000199:Actins; D003598:Cytoskeletal Proteins; D020409:Molecular Motor Proteins