Protein friction and filament bending facilitate contraction of disordered actomyosin networks

Alexander K.Y. Tam, Alex Mogilner, Dietmar B. Oelz

Research output: Contribution to journalArticlepeer-review


We use mathematical modeling and computation to investigate how protein friction facilitates contraction of disordered actomyosin networks. We simulate two-dimensional networks using an agent-based model, consisting of a system of force-balance equations for myosin motor proteins and semiflexible actin filaments. A major advantage of our approach is that it enables direct calculation of the network stress tensor, which provides a quantitative measure of contractility. Exploiting this, we use repeated simulations of disordered networks to confirm that both protein friction and actin filament bending are required for contraction. We then use simulations of elementary two-filament systems to show that filament bending flexibility can facilitate contraction on the microscopic scale. Finally, we show that actin filament turnover is necessary to sustain contraction and prevent filament aggregation. Simulations with and without turnover also exhibit contractile pulses. However, these pulses are aperiodic, suggesting that periodic pulsation can only arise because of additional regulatory mechanisms or more complex mechanical behavior.

Original languageEnglish (US)
Pages (from-to)4029-4040
Number of pages12
JournalBiophysical journal
Issue number18
StatePublished - Sep 21 2021

ASJC Scopus subject areas

  • Biophysics


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