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Motor activity dependent and independent functions for Myosin II in cytokinesis contribute to actomyosin ring assembly and contraction in Schizosaccharomyces pombe
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Palani, S., Chew, Ting Gang, Ramanujam, Srinivasan, Kamnev, Anton, Harne, Shrikant, Chapa y Lazo, Bernardo, Hogg, Rebecca, Sevugan, Mayalagu, Mishra, Mithilesh, Gayathri, Pananghat and Balasubramanian, Mohan K. (2017) Motor activity dependent and independent functions for Myosin II in cytokinesis contribute to actomyosin ring assembly and contraction in Schizosaccharomyces pombe. Current Biology, 27 (5). pp. 751-757. doi:10.1016/j.cub.2017.01.028 ISSN 0960-9822.
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WRAP-motor-activity-dependent-independent-functions-Myosin-II-Balasubramanian-2017.pdf - Published Version - Requires a PDF viewer. Available under License Creative Commons Attribution 4.0. Download (2989Kb) | Preview |
Official URL: https://doi.org/10.1016/j.cub.2017.01.028
Abstract
Cytokinesis depends on a contractile actomyosin ring in many eukaryotes [1, 2, 3]. Myosin II is a key component of the actomyosin ring, although whether it functions as a motor or as an actin cross-linker to exert its essential role is disputed [1, 4, 5]. In Schizosaccharomyces pombe, the myo2-E1 mutation affects the upper 50 kDa sub-domain of the myosin II heavy chain, and cells carrying this lethal mutation are defective in actomyosin ring assembly at the non-permissive temperature [6, 7]. myo2-E1 also affects actomyosin ring contraction when rings isolated from permissive temperature-grown cells are incubated with ATP [8]. Here we report isolation of a compensatory suppressor mutation in the lower 50 kDa sub-domain (myo2-E1-Sup1) that reverses the inability of myo2-E1 to form colonies at the restrictive temperature. myo2-E1-Sup1 is capable of assembling normal actomyosin rings, although rings isolated from myo2-E1-Sup1 are defective in ATP-dependent contraction in vitro. Furthermore, the product of myo2-E1-Sup1 does not translocate actin filaments in motility assays in vitro. Superimposition of myo2-E1 and myo2-E1-Sup1 on available rigor and blebbistatin-bound myosin II structures suggests that myo2-E1-Sup1 may represent a novel actin translocation-defective allele. Actomyosin ring contraction and viability of myo2-E1-Sup1 cells depend on the late cytokinetic S. pombe myosin II isoform, Myp2p, a non-essential protein that is normally dispensable for actomyosin ring assembly and contraction. Our work reveals that Myo2p may function in two different and essential modes during cytokinesis: a motor activity-independent form that can promote actomyosin ring assembly and a motor activity-dependent form that supports ring contraction.
Item Type: | Journal Article | |||||||||||||||||||||||||||
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Subjects: | Q Science > QH Natural history Q Science > QK Botany |
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Divisions: | Faculty of Science, Engineering and Medicine > Medicine > Warwick Medical School > Biomedical Sciences > Cell & Developmental Biology 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): | Cytokinesis, Schizosaccharomyces, Mutation (Biology) | |||||||||||||||||||||||||||
Journal or Publication Title: | Current Biology | |||||||||||||||||||||||||||
Publisher: | Cell Press | |||||||||||||||||||||||||||
ISSN: | 0960-9822 | |||||||||||||||||||||||||||
Official Date: | 6 March 2017 | |||||||||||||||||||||||||||
Dates: |
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Volume: | 27 | |||||||||||||||||||||||||||
Number: | 5 | |||||||||||||||||||||||||||
Page Range: | pp. 751-757 | |||||||||||||||||||||||||||
DOI: | 10.1016/j.cub.2017.01.028 | |||||||||||||||||||||||||||
Status: | Peer Reviewed | |||||||||||||||||||||||||||
Publication Status: | Published | |||||||||||||||||||||||||||
Access rights to Published version: | Open Access (Creative Commons) | |||||||||||||||||||||||||||
Date of first compliant deposit: | 15 May 2018 | |||||||||||||||||||||||||||
Date of first compliant Open Access: | 15 May 2018 | |||||||||||||||||||||||||||
RIOXX Funder/Project Grant: |
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