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Equatorial assembly of the cell-division actomyosin ring in the absence of cytokinetic spatial cues
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Lim, Tzer Chyn, Hatano, Tomoyuki, Kamnev, Anton, Balasubramanian, Mohan K. and Chew, Ting Gang (2018) Equatorial assembly of the cell-division actomyosin ring in the absence of cytokinetic spatial cues. Current Biology, 28 (6). pp. 955-962. e3. doi:10.1016/j.cub.2018.01.088 ISSN 1879-0445.
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WRAP-Equitorial-assembly-of-the-cell-division-acotmyosin-Lim-2018.pdf - Published Version - Requires a PDF viewer. Available under License Creative Commons Attribution 4.0. Download (3837Kb) | Preview |
Official URL: http://dx.doi.org/10.1016/j.cub.2018.01.088
Abstract
The position of the division site dictates the size and fate of daughter cells in many organisms. In animal cells, division-site placement involves overlapping mechanisms, including signaling from the central spindle microtubules, astral microtubules, and spindle poles and through polar contractions [1, 2, 3]. In fission yeast, division-site positioning requires overlapping mechanisms involving the anillin-related protein Mid1 and the tip complex (comprising the Kelch-repeat protein Tea1, the Dyrk-kinase Pom1, and the SH3-domain protein Tea4) [4, 5, 6, 7, 8, 9, 10, 11]. In addition to these factors, cell shape has also been shown to participate in the maintenance of the position of the actomyosin ring [12, 13, 14]. The first principles guiding actomyosin ring placement, however, have not been elucidated in any organism. Because actomyosin ring positioning, ring assembly, and cell morphogenesis are genetically separable in fission yeast, we have used it to derive actomyosin ring placement mechanisms from first principles. We report that, during ring assembly in the absence of cytokinetic cues (anillin-related Mid1 and tip-complex proteins), actin bundles follow the path of least curvature and assemble actomyosin rings in an equatorial position in spherical protoplasts and along the long axis in cylindrical cells and compressed protoplasts. The equatorial position of rings is abolished upon treatment of protoplasts with an actin-severing compound or by slowing down actin polymerization. We propose that the physical properties of actin filaments/bundles play key roles in actomyosin ring assembly and positioning, and that key cytokinetic molecules may modulate the length of actin filaments to promote ring assembly along the short axis.
| Item Type: | Journal Article | |||||||||||||||
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| Subjects: | Q Science > QH Natural history | |||||||||||||||
| Divisions: | Faculty of Science, Engineering and Medicine > Medicine > Warwick Medical School > Biomedical Sciences Faculty of Science, Engineering and Medicine > Medicine > Warwick Medical School |
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| Library of Congress Subject Headings (LCSH): | Spindle (Cell division), Actomyosin, Protoplasts | |||||||||||||||
| Journal or Publication Title: | Current Biology | |||||||||||||||
| Publisher: | Cell Press | |||||||||||||||
| ISSN: | 1879-0445 | |||||||||||||||
| Official Date: | 19 February 2018 | |||||||||||||||
| Dates: |
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| Volume: | 28 | |||||||||||||||
| Number: | 6 | |||||||||||||||
| Page Range: | pp. 955-962 | |||||||||||||||
| Article Number: | e3 | |||||||||||||||
| DOI: | 10.1016/j.cub.2018.01.088 | |||||||||||||||
| Status: | Peer Reviewed | |||||||||||||||
| Publication Status: | Published | |||||||||||||||
| Access rights to Published version: | Open Access (Creative Commons) | |||||||||||||||
| Date of first compliant deposit: | 12 September 2019 | |||||||||||||||
| Date of first compliant Open Access: | 12 September 2019 | |||||||||||||||
| RIOXX Funder/Project Grant: |
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