PMID:
28655757
DOI:
10.1083/jcb.201701104
Author(s):
Chew, Ting Gang, Huang, Junqi, Palani, Saravanan, Sommese, Ruth, Kamnev, Anton, Hatano, Tomoyuki, Gu, Ying, Oliferenko, Snezhana, Sivaramakrishnan, Sivaraj, Balasubramanian, Mohan K
Publisher(s):
Rockefeller University Press
Tags:
Biochemistry, Genetics and Molecular Biology
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article description
Cytokinesis in many eukaryotes involves a tension-generating actomyosin-based contractile ring. Many components of actomyosin rings turn over during contraction, although the significance of this turnover has remained enigmatic. Here, using , we investigate the role of turnover of actin and myosin II in its contraction. Actomyosin ring components self-organize into ∼1-µm-spaced clusters instead of undergoing full-ring contraction in the absence of continuous actin polymerization. This effect is reversed when actin filaments are stabilized. We tested the idea that the function of turnover is to ensure actin filament homeostasis in a synthetic system, in which we abolished turnover by fixing rings in cell ghosts with formaldehyde. We found that these rings contracted fully upon exogenous addition of a vertebrate myosin. We conclude that actin turnover is required to maintain actin filament homeostasis during ring contraction and that the requirement for turnover can be bypassed if homeostasis is achieved artificially.

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