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dc.contributor.authorGrallert, Agnes
dc.contributor.authorConnolly, Yvonne
dc.contributor.authorSmith, Duncan L
dc.contributor.authorSimanis, Viesturs
dc.contributor.authorHagan, Iain M
dc.date.accessioned2012-11-09T14:50:10Z
dc.date.available2012-11-09T14:50:10Z
dc.date.issued2012-07
dc.identifier.citationThe S. pombe cytokinesis NDR kinase Sid2 activates Fin1 NIMA kinase to control mitotic commitment through Pom1/Wee1. 2012, 14 (7):738-45 Nat Cell Biolen_GB
dc.identifier.issn1476-4679
dc.identifier.pmid22684255
dc.identifier.doi10.1038/ncb2514
dc.identifier.urihttp://hdl.handle.net/10541/251567
dc.description.abstractMitotic exit integrates the reversal of the phosphorylation events initiated by mitotic kinases with a controlled cytokinesis event that cleaves the cell in two. The mitotic exit network (MEN) of budding yeast regulates both processes, whereas the fission yeast equivalent, the septum initiation network (SIN), controls only the execution of cytokinesis. The components and architecture of the SIN and MEN are highly conserved. At present, it is assumed that the functions of the core SIN-MEN components are restricted to their characterized roles at the end of mitosis. We now show that the NDR (nuclear Dbf2-related) kinase component of the fission yeast SIN, Sid2-Mob1, acts independently of the other known SIN components in G2 phase of the cell cycle to control the timing of mitotic commitment. Sid2-Mob1 promotes mitotic commitment by directly activating the NIMA (Never In Mitosis)-related kinase Fin1. Fin1's activation promotes its own destruction, thereby making Fin1 activation a transient feature of G2 phase. This spike of Fin1 activation modulates the activity of the Pom1/Cdr1/Cdr2 geometry network towards Wee1.
dc.language.isoenen
dc.rightsArchived with thanks to Nature cell biologyen_GB
dc.subject.meshCell Cycle Proteins
dc.subject.meshCytokinesis
dc.subject.meshCytoskeletal Proteins
dc.subject.meshEnzyme Activation
dc.subject.meshEnzyme Inhibitors
dc.subject.meshG2 Phase
dc.subject.meshMitosis
dc.subject.meshMutation
dc.subject.meshNuclear Proteins
dc.subject.meshPhosphorylation
dc.subject.meshProtein Kinases
dc.subject.meshProtein-Serine-Threonine Kinases
dc.subject.meshProtein-Tyrosine Kinases
dc.subject.meshSaccharomyces cerevisiae Proteins
dc.subject.meshSchizosaccharomyces
dc.subject.meshSchizosaccharomyces pombe Proteins
dc.subject.meshSerine
dc.subject.meshSignal Transduction
dc.subject.meshTime Factors
dc.titleThe S. pombe cytokinesis NDR kinase Sid2 activates Fin1 NIMA kinase to control mitotic commitment through Pom1/Wee1.en
dc.typeArticleen
dc.contributor.departmentCRUK Cell Division Group, Paterson Institute for Cancer Research, Wilmslow Road, Manchester M20 4BX, UK.en_GB
dc.identifier.journalNature Cell Biologyen_GB
refterms.dateFOA2020-04-21T10:04:07Z
html.description.abstractMitotic exit integrates the reversal of the phosphorylation events initiated by mitotic kinases with a controlled cytokinesis event that cleaves the cell in two. The mitotic exit network (MEN) of budding yeast regulates both processes, whereas the fission yeast equivalent, the septum initiation network (SIN), controls only the execution of cytokinesis. The components and architecture of the SIN and MEN are highly conserved. At present, it is assumed that the functions of the core SIN-MEN components are restricted to their characterized roles at the end of mitosis. We now show that the NDR (nuclear Dbf2-related) kinase component of the fission yeast SIN, Sid2-Mob1, acts independently of the other known SIN components in G2 phase of the cell cycle to control the timing of mitotic commitment. Sid2-Mob1 promotes mitotic commitment by directly activating the NIMA (Never In Mitosis)-related kinase Fin1. Fin1's activation promotes its own destruction, thereby making Fin1 activation a transient feature of G2 phase. This spike of Fin1 activation modulates the activity of the Pom1/Cdr1/Cdr2 geometry network towards Wee1.


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