A Combination of Actin Treadmilling and Cross-Linking Drives Contraction of Random Actomyosin Arrays.

ABSTRACT: We investigate computationally the self-organization and contraction of an initially random actomyosin ring. In the framework of a detailed physical model for a ring of cross-linked actin filaments and myosin-II clusters, we derive the force balance equations and solve them numerically. We find that to contract, actin filaments have to treadmill and to be sufficiently cross linked, and myosin has to be processive. The simulations reveal how contraction scales with mechanochemical parameters. For example, they show that the ring made of longer filaments generates greater force but contracts slower. The model predicts that the ring contracts with a constant rate proportional to the initial ring radius if either myosin is released from the ring during contraction and actin filaments shorten,

SUBMITTER: Oelz DB 

PROVIDER: S-EPMC4643270 | biostudies-literature | 2015 Nov

REPOSITORIES: biostudies-literature