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Cdk1 promotes cytokinesis in fission yeast through activation of the septation initiation network
In Schizosaccharomyces pombe, late mitotic events are coordinated with cytokinesis by the septation initiation network (SIN), an essential spindle pole body (SPB)–associated kinase cascade, which controls the formation, maintenance, and constriction of the cytokinetic ring. It is not fully understoo...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The American Society for Cell Biology
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4116299/ https://www.ncbi.nlm.nih.gov/pubmed/24920823 http://dx.doi.org/10.1091/mbc.E14-04-0936 |
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author | Rachfall, Nicole Johnson, Alyssa E. Mehta, Sapna Chen, Jun-Song Gould, Kathleen L. |
author_facet | Rachfall, Nicole Johnson, Alyssa E. Mehta, Sapna Chen, Jun-Song Gould, Kathleen L. |
author_sort | Rachfall, Nicole |
collection | PubMed |
description | In Schizosaccharomyces pombe, late mitotic events are coordinated with cytokinesis by the septation initiation network (SIN), an essential spindle pole body (SPB)–associated kinase cascade, which controls the formation, maintenance, and constriction of the cytokinetic ring. It is not fully understood how SIN initiation is temporally regulated, but it depends on the activation of the GTPase Spg1, which is inhibited during interphase by the essential bipartite GTPase-activating protein Byr4-Cdc16. Cells are particularly sensitive to the modulation of Byr4, which undergoes cell cycle–dependent phosphorylation presumed to regulate its function. Polo-like kinase, which promotes SIN activation, is partially responsible for Byr4 phosphorylation. Here we show that Byr4 is also controlled by cyclin-dependent kinase (Cdk1)–mediated phosphorylation. A Cdk1 nonphosphorylatable Byr4 phosphomutant displays severe cell division defects, including the formation of elongated, multinucleate cells, failure to maintain the cytokinetic ring, and compromised SPB association of the SIN kinase Cdc7. Our analyses show that Cdk1-mediated phosphoregulation of Byr4 facilitates complete removal of Byr4 from metaphase SPBs in concert with Plo1, revealing an unexpected role for Cdk1 in promoting cytokinesis through activation of the SIN pathway. |
format | Online Article Text |
id | pubmed-4116299 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-41162992014-10-16 Cdk1 promotes cytokinesis in fission yeast through activation of the septation initiation network Rachfall, Nicole Johnson, Alyssa E. Mehta, Sapna Chen, Jun-Song Gould, Kathleen L. Mol Biol Cell Articles In Schizosaccharomyces pombe, late mitotic events are coordinated with cytokinesis by the septation initiation network (SIN), an essential spindle pole body (SPB)–associated kinase cascade, which controls the formation, maintenance, and constriction of the cytokinetic ring. It is not fully understood how SIN initiation is temporally regulated, but it depends on the activation of the GTPase Spg1, which is inhibited during interphase by the essential bipartite GTPase-activating protein Byr4-Cdc16. Cells are particularly sensitive to the modulation of Byr4, which undergoes cell cycle–dependent phosphorylation presumed to regulate its function. Polo-like kinase, which promotes SIN activation, is partially responsible for Byr4 phosphorylation. Here we show that Byr4 is also controlled by cyclin-dependent kinase (Cdk1)–mediated phosphorylation. A Cdk1 nonphosphorylatable Byr4 phosphomutant displays severe cell division defects, including the formation of elongated, multinucleate cells, failure to maintain the cytokinetic ring, and compromised SPB association of the SIN kinase Cdc7. Our analyses show that Cdk1-mediated phosphoregulation of Byr4 facilitates complete removal of Byr4 from metaphase SPBs in concert with Plo1, revealing an unexpected role for Cdk1 in promoting cytokinesis through activation of the SIN pathway. The American Society for Cell Biology 2014-08-01 /pmc/articles/PMC4116299/ /pubmed/24920823 http://dx.doi.org/10.1091/mbc.E14-04-0936 Text en © 2014 Rachfall et al. 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 (http://creativecommons.org/licenses/by-nc-sa/3.0). “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society of Cell Biology. |
spellingShingle | Articles Rachfall, Nicole Johnson, Alyssa E. Mehta, Sapna Chen, Jun-Song Gould, Kathleen L. Cdk1 promotes cytokinesis in fission yeast through activation of the septation initiation network |
title | Cdk1 promotes cytokinesis in fission yeast through activation of the septation
initiation network |
title_full | Cdk1 promotes cytokinesis in fission yeast through activation of the septation
initiation network |
title_fullStr | Cdk1 promotes cytokinesis in fission yeast through activation of the septation
initiation network |
title_full_unstemmed | Cdk1 promotes cytokinesis in fission yeast through activation of the septation
initiation network |
title_short | Cdk1 promotes cytokinesis in fission yeast through activation of the septation
initiation network |
title_sort | cdk1 promotes cytokinesis in fission yeast through activation of the septation
initiation network |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4116299/ https://www.ncbi.nlm.nih.gov/pubmed/24920823 http://dx.doi.org/10.1091/mbc.E14-04-0936 |
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