Stress generation and filament turnover during actin ring constriction.
We present a physical analysis of the dynamics and mechanics of contractile actin rings. In particular, we analyze the dynamics of ring contraction during cytokinesis in the Caenorhabditis elegans embryo. We present a general analysis of force balances and material exchange and estimate the relevant parameter values. We show that on a microscopic level contractile stresses can result from both the action of motor proteins, which cross-link filaments, and from the polymerization and depolymerization of filaments in the presence of end-tracking cross-linkers.
Max Planck Institute for the Physics of Complex Systems, Dresden, Germany.
Alexander
A
Zumdieck
Karsten
K
Kruse
Henrik
H
Bringmann
Anthony A
AA
Hyman
Frank
F
Jülicher
D008841:Actin Cytoskeleton / Q000378:metabolism* / Q000648:ultrastructure; D000818:Animals; D017173:Caenorhabditis elegans / Q000166:cytology / Q000196:embryology; D048749:Cytokinesis / Q000502:physiology*; D003599:Cytoskeleton / Q000378:metabolism* / Q000648:ultrastructure; D004625:Embryo, Nonmammalian / Q000166:cytology / Q000378:metabolism; D008962:Models, Theoretical; D020409:Molecular Motor Proteins / Q000378:metabolism; D024462:Myosin Type II / Q000235:genetics / Q000378:metabolism; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000378:metabolism; D013314:Stress, Mechanical
D020409:Molecular Motor Proteins; D011993:Recombinant Fusion Proteins; D024462:Myosin Type II