Myosin-driven actin-microtubule networks exhibit self-organized contractile dynamics

Gloria Lee, Gregor Leech, Michael J. Rust, Moumita Das, Ryan J. McGorty, Jennifer L. Ross, Rae M. Robertson-Anderson

Research output: Contribution to journalArticlepeer-review

Abstract

The cytoskeleton is a dynamic network of proteins, including actin, microtubules, and their associated motor proteins, that enables essential cellular processes such as motility, division, and growth. While actomyosin networks are extensively studied, how interactions between actin and microtubules, ubiquitous in the cytoskeleton, influence actomyosin activity remains an open question. Here, we create a network of co-entangled actin and microtubules driven by myosin II. We combine dynamic differential microscopy, particle image velocimetry, and particle tracking to show that both actin and microtubules undergo ballistic contraction with unexpectedly indistinguishable characteristics. This contractility is distinct from faster disordered motion and rupturing that active actin networks exhibit. Our results suggest that microtubules enable self-organized myosin-driven contraction by providing flexural rigidity and enhanced connectivity to actin networks. Beyond the immediate relevance to cytoskeletal dynamics, our results shed light on the design of active materials that can be precisely tuned by the network composition.

Original languageEnglish (US)
Article numbereabe4334
JournalScience Advances
Volume7
Issue number6
DOIs
StatePublished - Feb 5 2021

ASJC Scopus subject areas

  • General

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