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

Dietmar B. Oelz, Boris Y. Rubinstein, Alex Mogilner

Research output: Contribution to journalArticlepeer-review

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, or if myosin is retained in the ring, while the actin filament number decreases. We demonstrate that a balance of actin nucleation and compression-dependent disassembly can also sustain contraction. Finally, the model demonstrates that with time pattern formation takes place in the ring, worsening the contractile process. The more random the actin dynamics are, the higher the contractility will be.

Original languageEnglish (US)
Pages (from-to)1818-1829
Number of pages12
JournalBiophysical journal
Volume109
Issue number9
DOIs
StatePublished - Nov 3 2015

ASJC Scopus subject areas

  • Biophysics

Fingerprint Dive into the research topics of 'A Combination of Actin Treadmilling and Cross-Linking Drives Contraction of Random Actomyosin Arrays'. Together they form a unique fingerprint.

Cite this