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The ARP2/3 complex prevents excessive formin activity during cytokinesis
Cytokinesis completes cell division by constriction of an actomyosin contractile ring that separates the two daughter cells. Here we use the early Caenorhabditis elegans embryo to explore how the actin filament network in the ring and the surrounding cortex is regulated by the single cytokinesis for...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The American Society for Cell Biology
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6337913/ https://www.ncbi.nlm.nih.gov/pubmed/30403552 http://dx.doi.org/10.1091/mbc.E18-07-0471 |
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author | Chan, Fung-Yi Silva, Ana M. Saramago, Joana Pereira-Sousa, Joana Brighton, Hailey E. Pereira, Marisa Oegema, Karen Gassmann, Reto Carvalho, Ana Xavier |
author_facet | Chan, Fung-Yi Silva, Ana M. Saramago, Joana Pereira-Sousa, Joana Brighton, Hailey E. Pereira, Marisa Oegema, Karen Gassmann, Reto Carvalho, Ana Xavier |
author_sort | Chan, Fung-Yi |
collection | PubMed |
description | Cytokinesis completes cell division by constriction of an actomyosin contractile ring that separates the two daughter cells. Here we use the early Caenorhabditis elegans embryo to explore how the actin filament network in the ring and the surrounding cortex is regulated by the single cytokinesis formin CYK-1 and the ARP2/3 complex, which nucleate nonbranched and branched filaments, respectively. We show that CYK-1 and the ARP2/3 complex are the predominant F-actin nucleators responsible for generating distinct cortical F-actin architectures and that depletion of either nucleator affects the kinetics of cytokinesis. CYK-1 is critical for normal F-actin levels in the contractile ring, and acute inhibition of CYK-1 after furrow ingression slows ring constriction rate, suggesting that CYK-1 activity is required throughout ring constriction. Surprisingly, although the ARP2/3 complex does not localize in the contractile ring, depletion of the ARP2 subunit or treatment with ARP2/3 complex inhibitor delays contractile ring formation and constriction. We present evidence that the delays are due to an excess in formin-nucleated cortical F-actin, suggesting that the ARP2/3 complex negatively regulates CYK-1 activity. We conclude that the kinetics of cytokinesis are modulated by interplay between the two major actin filament nucleators. |
format | Online Article Text |
id | pubmed-6337913 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-63379132019-03-16 The ARP2/3 complex prevents excessive formin activity during cytokinesis Chan, Fung-Yi Silva, Ana M. Saramago, Joana Pereira-Sousa, Joana Brighton, Hailey E. Pereira, Marisa Oegema, Karen Gassmann, Reto Carvalho, Ana Xavier Mol Biol Cell Articles Cytokinesis completes cell division by constriction of an actomyosin contractile ring that separates the two daughter cells. Here we use the early Caenorhabditis elegans embryo to explore how the actin filament network in the ring and the surrounding cortex is regulated by the single cytokinesis formin CYK-1 and the ARP2/3 complex, which nucleate nonbranched and branched filaments, respectively. We show that CYK-1 and the ARP2/3 complex are the predominant F-actin nucleators responsible for generating distinct cortical F-actin architectures and that depletion of either nucleator affects the kinetics of cytokinesis. CYK-1 is critical for normal F-actin levels in the contractile ring, and acute inhibition of CYK-1 after furrow ingression slows ring constriction rate, suggesting that CYK-1 activity is required throughout ring constriction. Surprisingly, although the ARP2/3 complex does not localize in the contractile ring, depletion of the ARP2 subunit or treatment with ARP2/3 complex inhibitor delays contractile ring formation and constriction. We present evidence that the delays are due to an excess in formin-nucleated cortical F-actin, suggesting that the ARP2/3 complex negatively regulates CYK-1 activity. We conclude that the kinetics of cytokinesis are modulated by interplay between the two major actin filament nucleators. The American Society for Cell Biology 2019-01-01 /pmc/articles/PMC6337913/ /pubmed/30403552 http://dx.doi.org/10.1091/mbc.E18-07-0471 Text en © 2019 Chan 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. http://creativecommons.org/licenses/by-nc-sa/3.0 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 3.0 Unported Creative Commons License. |
spellingShingle | Articles Chan, Fung-Yi Silva, Ana M. Saramago, Joana Pereira-Sousa, Joana Brighton, Hailey E. Pereira, Marisa Oegema, Karen Gassmann, Reto Carvalho, Ana Xavier The ARP2/3 complex prevents excessive formin activity during cytokinesis |
title | The ARP2/3 complex prevents excessive formin activity during cytokinesis |
title_full | The ARP2/3 complex prevents excessive formin activity during cytokinesis |
title_fullStr | The ARP2/3 complex prevents excessive formin activity during cytokinesis |
title_full_unstemmed | The ARP2/3 complex prevents excessive formin activity during cytokinesis |
title_short | The ARP2/3 complex prevents excessive formin activity during cytokinesis |
title_sort | arp2/3 complex prevents excessive formin activity during cytokinesis |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6337913/ https://www.ncbi.nlm.nih.gov/pubmed/30403552 http://dx.doi.org/10.1091/mbc.E18-07-0471 |
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