Cargando…

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...

Descripción completa

Detalles Bibliográficos
Autores principales: Rachfall, Nicole, Johnson, Alyssa E., Mehta, Sapna, Chen, Jun-Song, Gould, Kathleen L.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The American Society for Cell Biology 2014
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
_version_ 1782328592433152000
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
work_keys_str_mv AT rachfallnicole cdk1promotescytokinesisinfissionyeastthroughactivationoftheseptationinitiationnetwork
AT johnsonalyssae cdk1promotescytokinesisinfissionyeastthroughactivationoftheseptationinitiationnetwork
AT mehtasapna cdk1promotescytokinesisinfissionyeastthroughactivationoftheseptationinitiationnetwork
AT chenjunsong cdk1promotescytokinesisinfissionyeastthroughactivationoftheseptationinitiationnetwork
AT gouldkathleenl cdk1promotescytokinesisinfissionyeastthroughactivationoftheseptationinitiationnetwork