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Myosin turnover controls actomyosin contractile instability
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Thiyagarajan, Sathish, Wang, Shuyuan, Chew, Ting Gang, Huang, Junqi, Kumar, Lokesh, Balasubramanian, Mohan K. and O’Shaughnessy, Ben (2022) Myosin turnover controls actomyosin contractile instability. Proceedings of the National Academy of Sciences of the United States of America, 119 (43). e2211431119. doi:10.1073/pnas.2211431119 ISSN 0027-8424.
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Official URL: https://doi.org/10.1073/pnas.2211431119
Abstract
Actomyosin contractile force produced by myosin II molecules that bind and pull actin filaments is harnessed for diverse functions, from cell division by the cytokinetic contractile ring to morphogenesis driven by supracellular actomyosin networks during development. However, actomyosin contractility is intrinsically unstable to self-reinforcing spatial variations that may destroy the actomyosin architecture if unopposed. How cells control this threat is not established, and while large myosin fluctuations and punctateness are widely reported, the full course of the instability in cells has not been observed. Here, we observed the instability run its full course in isolated cytokinetic contractile rings in cell ghosts where component turnover processes are absent. Unprotected by turnover, myosin II merged hierarchically into aggregates with increasing amounts of myosin and increasing separation, up to a maximum separation. Molecularly explicit simulations reproduced the hierarchical aggregation which precipitated tension loss and ring fracture and identified the maximum separation as the length of actin filaments mediating mechanical communication between aggregates. In the final simulated dead-end state, aggregates were morphologically quiescent, including asters with polarity-sorted actin, similar to the dead-end state observed in actomyosin systems in vitro. Our results suggest the myosin II turnover time controls actomyosin contractile instability in normal cells, long enough for aggregation to build robust aggregates but sufficiently short to intercept catastrophic hierarchical aggregation and fracture.
Item Type: | Journal Article | |||||||||
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Subjects: | Q Science > QH Natural history Q Science > QP Physiology |
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Divisions: | Faculty of Science, Engineering and Medicine > Medicine > Warwick Medical School | |||||||||
SWORD Depositor: | Library Publications Router | |||||||||
Library of Congress Subject Headings (LCSH): | Myosin , Actomyosin , Cytokinesis , Cell division | |||||||||
Journal or Publication Title: | Proceedings of the National Academy of Sciences of the United States of America | |||||||||
Publisher: | National Academy of Sciences | |||||||||
ISSN: | 0027-8424 | |||||||||
Official Date: | 25 September 2022 | |||||||||
Dates: |
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Volume: | 119 | |||||||||
Number: | 43 | |||||||||
Number of Pages: | 12 | |||||||||
Article Number: | e2211431119 | |||||||||
DOI: | 10.1073/pnas.2211431119 | |||||||||
Status: | Peer Reviewed | |||||||||
Publication Status: | Published | |||||||||
Access rights to Published version: | Open Access (Creative Commons) | |||||||||
Date of first compliant deposit: | 9 November 2022 | |||||||||
Date of first compliant Open Access: | 10 November 2022 | |||||||||
RIOXX Funder/Project Grant: |
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