Koenderink, GH;
Paluch, EK;
(2018)
Architecture shapes contractility in actomyosin networks.
Current Opinion in Cell Biology
, 50
pp. 79-85.
10.1016/j.ceb.2018.01.015.
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Abstract
Myosin-driven contraction of the actin cytoskeleton is at the base of cell and tissue morphogenesis. At the molecular level, myosin motors drive contraction by sliding actin filaments past one another using energy produced by ATP hydrolysis. How this microscopic sliding activity gives rise to cell-scale contractions has been an active research question first in muscle cells, and over the last few decades in non-muscle cells. While many early investigations focused on myosin motor activity, increasingly, the nanoscale architecture of the actin network emerges as a key regulator of contractility. Here we review theoretical and in vitro reconstitution studies that have uncovered some of the key mechanisms by which actin network organization controls contractile tension generation. We then discuss recent findings indicating that similar principles apply in cells.
Type: | Article |
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Title: | Architecture shapes contractility in actomyosin networks |
Location: | England |
Open access status: | An open access version is available from UCL Discovery |
DOI: | 10.1016/j.ceb.2018.01.015 |
Publisher version: | https://doi.org/10.1016/j.ceb.2018.01.015 |
Language: | English |
Additional information: | This version is the author accepted manuscript. For information on re-use, please refer to the publisher’s terms and conditions. |
UCL classification: | UCL UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Lab for Molecular Cell Bio MRC-UCL |
URI: | https://discovery.ucl.ac.uk/id/eprint/10049319 |
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