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Counting actin in contractile rings reveals novel contributions of cofilin and type II myosins to fission yeast cytokinesis
Cytokinesis by animals, fungi, and amoebas depends on actomyosin contractile rings, which are stabilized by continuous turnover of actin filaments. Remarkably little is known about the amount of polymerized actin in contractile rings, so we used low concentrations of GFP-Lifeact to count total polym...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The American Society for Cell Biology
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9265160/ https://www.ncbi.nlm.nih.gov/pubmed/34613787 http://dx.doi.org/10.1091/mbc.E21-08-0376 |
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author | Malla, Mamata Pollard, Thomas D. Chen, Qian |
author_facet | Malla, Mamata Pollard, Thomas D. Chen, Qian |
author_sort | Malla, Mamata |
collection | PubMed |
description | Cytokinesis by animals, fungi, and amoebas depends on actomyosin contractile rings, which are stabilized by continuous turnover of actin filaments. Remarkably little is known about the amount of polymerized actin in contractile rings, so we used low concentrations of GFP-Lifeact to count total polymerized actin molecules in the contractile rings of live fission yeast cells. Contractile rings of wild-type cells accumulated polymerized actin molecules at 4900/min to a peak number of ∼198,000 followed by a loss of actin at 5400/min throughout ring constriction. In adf1-M3 mutant cells with cofilin that severs actin filaments poorly, contractile rings accumulated polymerized actin at twice the normal rate and eventually had almost twofold more actin along with a proportional increase in type II myosins Myo2, Myp2, and formin Cdc12. Although 30% of adf1-M3 mutant cells failed to constrict their rings fully, the rest lost actin from the rings at the wild-type rates. Mutations of type II myosins Myo2 and Myp2 reduced contractile ring actin filaments by half and slowed the rate of actin loss from the rings. |
format | Online Article Text |
id | pubmed-9265160 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-92651602022-07-27 Counting actin in contractile rings reveals novel contributions of cofilin and type II myosins to fission yeast cytokinesis Malla, Mamata Pollard, Thomas D. Chen, Qian Mol Biol Cell Articles Cytokinesis by animals, fungi, and amoebas depends on actomyosin contractile rings, which are stabilized by continuous turnover of actin filaments. Remarkably little is known about the amount of polymerized actin in contractile rings, so we used low concentrations of GFP-Lifeact to count total polymerized actin molecules in the contractile rings of live fission yeast cells. Contractile rings of wild-type cells accumulated polymerized actin molecules at 4900/min to a peak number of ∼198,000 followed by a loss of actin at 5400/min throughout ring constriction. In adf1-M3 mutant cells with cofilin that severs actin filaments poorly, contractile rings accumulated polymerized actin at twice the normal rate and eventually had almost twofold more actin along with a proportional increase in type II myosins Myo2, Myp2, and formin Cdc12. Although 30% of adf1-M3 mutant cells failed to constrict their rings fully, the rest lost actin from the rings at the wild-type rates. Mutations of type II myosins Myo2 and Myp2 reduced contractile ring actin filaments by half and slowed the rate of actin loss from the rings. The American Society for Cell Biology 2022-05-12 /pmc/articles/PMC9265160/ /pubmed/34613787 http://dx.doi.org/10.1091/mbc.E21-08-0376 Text en © 2022 Malla et al. “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society for Cell Biology. https://creativecommons.org/licenses/by-nc-sa/4.0/This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial-Share Alike 4.0 International Creative Commons License. |
spellingShingle | Articles Malla, Mamata Pollard, Thomas D. Chen, Qian Counting actin in contractile rings reveals novel contributions of cofilin and type II myosins to fission yeast cytokinesis |
title | Counting actin in contractile rings reveals novel contributions of cofilin and type II myosins to fission yeast cytokinesis |
title_full | Counting actin in contractile rings reveals novel contributions of cofilin and type II myosins to fission yeast cytokinesis |
title_fullStr | Counting actin in contractile rings reveals novel contributions of cofilin and type II myosins to fission yeast cytokinesis |
title_full_unstemmed | Counting actin in contractile rings reveals novel contributions of cofilin and type II myosins to fission yeast cytokinesis |
title_short | Counting actin in contractile rings reveals novel contributions of cofilin and type II myosins to fission yeast cytokinesis |
title_sort | counting actin in contractile rings reveals novel contributions of cofilin and type ii myosins to fission yeast cytokinesis |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9265160/ https://www.ncbi.nlm.nih.gov/pubmed/34613787 http://dx.doi.org/10.1091/mbc.E21-08-0376 |
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