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Constriction mechanism of the actomyosin ring

Nguyen, L. T. and Swulius, M. T. and Mishra, M. and Jensen, G. J. (2016) Constriction mechanism of the actomyosin ring. Molecular Biology of the Cell, 27 . Art. No. P1851. ISSN 1059-1524. http://resolver.caltech.edu/CaltechAUTHORS:20170331-135448715

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Abstract

Cytokinesis in most eukaryotic cells is orchestrated by a contractile actomyosin ring. While many of the proteins involved are known, the mechanism of constriction remains unclear. Based on the current literature and new 3D molecular details from electron cryotomography, here we developed 3D coarse‐grained models of actin filaments, unipolar and bipolar myosins, actin crosslinkers, and membranes and simulated their interactions. Exploring a matrix of possible actomyosin configurations showed that node‐based architectures like those presently described for ring assembly result in membrane puckers not seen in EM images of real cells. Instead, actin and myosin are more likely uniformly distributed around the ring. In the model that best matches data from fluorescence microscopy, electron cryotomography, and biochemical experiments, ring tension is generated by interactions between bipolar myosins and actin, and transmitted to the membrane via unipolar myosins.


Item Type:Article
Related URLs:
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http://www.ascb.org/2016meetingOrganizationConference Website
ORCID:
AuthorORCID
Jensen, G. J.0000-0003-1556-4864
Additional Information:© 2016 American Society for Cell Biology.
Record Number:CaltechAUTHORS:20170331-135448715
Persistent URL:http://resolver.caltech.edu/CaltechAUTHORS:20170331-135448715
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:75600
Collection:CaltechAUTHORS
Deposited By: Tony Diaz
Deposited On:01 Apr 2017 04:56
Last Modified:01 Apr 2017 04:56

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