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DOI10.1073/pnas.1920337117
Cleavage-furrow formation without F-actin in Chlamydomonas
Onishi M.; Umen J.G.; Cross F.R.; Pringle J.R.
发表日期2020
ISSN0027-8424
起始页码18511
结束页码18520
卷号117期号:31
英文摘要It is widely believed that cleavage-furrow formation during cytokinesis is driven by the contraction of a ring containing F-actin and type-II myosin. However, even in cells that have such rings, they are not always essential for furrow formation. Moreover, many taxonomically diverse eukaryotic cells divide by furrowing but have no type-II myosin, making it unlikely that an actomyosin ring drives furrowing. To explore this issue further, we have used one such organism, the green alga Chlamydomonas reinhardtii. We found that although F-actin is associated with the furrow region, none of the three myosins (of types VIII and XI) is localized there. Moreover, when F-actin was eliminated through a combination of a mutation and a drug, furrows still formed and the cells divided, although somewhat less efficiently than normal. Unexpectedly, division of the large Chlamydomonas chloroplast was delayed in the cells lacking F-actin; as this organelle lies directly in the path of the cleavage furrow, this delay may explain, at least in part, the delay in cytokinesis itself. Earlier studies had shown an association of microtubules with the cleavage furrow, and we used a fluorescently tagged EB1 protein to show that microtubules are still associated with the furrows in the absence of F-actin, consistent with the possibility that the microtubules are important for furrow formation. We suggest that the actomyosin ring evolved as one way to improve the efficiency of a core process for furrow formation that was already present in ancestral eukaryotes. © 2020 National Academy of Sciences. All rights reserved.
英文关键词Cell division; Chloroplast division; Cytokinesis; Microtubules; Myosin
语种英语
scopus关键词Article; cell membrane; Chlamydomonas reinhardtii; chloroplast; controlled study; cytokinesis; depolymerization; Dictyostelium; eukaryote; microtubule; Naegleria gruberi; nonhuman; phragmoplast; priority journal; protein analysis; protein cleavage; protein function; protein localization; Saccharomyces cerevisiae; actin filament; cell division; chemistry; Chlamydomonas; cytology; metabolism; actin; myosin; protein binding; Actin Cytoskeleton; Actins; Cell Division; Chlamydomonas; Cytokinesis; Microtubules; Myosins; Protein Binding
来源期刊Proceedings of the National Academy of Sciences of the United States of America
文献类型期刊论文
条目标识符http://gcip.llas.ac.cn/handle/2XKMVOVA/160243
作者单位Onishi, M., Department of Genetics, Stanford University School of Medicine, Stanford, CA 94305, United States, Department of Biology, Duke University, Durham, NC 27708, United States; Umen, J.G., Donald Danforth Plant Science Center, St. Louis, MO 63132, United States; Cross, F.R., Rockefeller University, New York, NY 10065, United States; Pringle, J.R., Department of Genetics, Stanford University School of Medicine, Stanford, CA 94305, United States
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GB/T 7714
Onishi M.,Umen J.G.,Cross F.R.,et al. Cleavage-furrow formation without F-actin in Chlamydomonas[J],2020,117(31).
APA Onishi M.,Umen J.G.,Cross F.R.,&Pringle J.R..(2020).Cleavage-furrow formation without F-actin in Chlamydomonas.Proceedings of the National Academy of Sciences of the United States of America,117(31).
MLA Onishi M.,et al."Cleavage-furrow formation without F-actin in Chlamydomonas".Proceedings of the National Academy of Sciences of the United States of America 117.31(2020).
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