Please use this identifier to cite or link to this item: https://doi.org/10.1371/journal.pone.0079001
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dc.titleCDK-dependent nuclear localization of B-cyclin Clb1 promotes FEAR activation during meiosis I in budding yeast
dc.contributor.authorTibbles K.L.
dc.contributor.authorSarkar S.
dc.contributor.authorNovak B.
dc.contributor.authorArumugam P.
dc.date.accessioned2019-11-04T06:31:57Z
dc.date.available2019-11-04T06:31:57Z
dc.date.issued2013
dc.identifier.citationTibbles K.L., Sarkar S., Novak B., Arumugam P. (2013). CDK-dependent nuclear localization of B-cyclin Clb1 promotes FEAR activation during meiosis I in budding yeast. PLoS ONE 8 (11) : e79001. ScholarBank@NUS Repository. https://doi.org/10.1371/journal.pone.0079001
dc.identifier.issn19326203
dc.identifier.urihttps://scholarbank.nus.edu.sg/handle/10635/161354
dc.description.abstractCyclin-dependent kinases (CDK) are master regulators of the cell cycle in eukaryotes. CDK activity is regulated by the presence, post-translational modification and spatial localization of its regulatory subunit cyclin. In budding yeast, the Bcyclin Clb1 is phosphorylated and localizes to the nucleus during meiosis I. However the functional significance of Clb1's phosphorylation and nuclear localization and their mutual dependency is unknown. In this paper, we demonstrate that meiosis-specific phosphorylation of Clb1 requires its import to the nucleus but not vice versa. While Clb1 phosphorylation is dependent on activity of both CDK and polo-like kinase Cdc5, its nuclear localization requires CDK but not Cdc5 activity. Furthermore we show that increased nuclear localization of Clb1 during meiosis enhances activation of FEAR (Cdc Fourteen Early Anaphase Release) pathway. We discuss the significance of our results in relation to regulation of exit from meiosis I. © 2013 Tibbles et al.
dc.rightsAttribution 4.0 International
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/
dc.sourceUnpaywall 20191101
dc.subjectcyclin B
dc.subjectcyclin dependent kinase
dc.subjectcyclin dependent kinase fourteen early anaphase release protein
dc.subjectphosphoprotein phosphatase Cdc14
dc.subjectpolo like kinase
dc.subjectprotein Cdc5
dc.subjectprotein Clb1
dc.subjectunclassified drug
dc.subjectarticle
dc.subjectcell nucleus
dc.subjectcellular distribution
dc.subjectcontrolled study
dc.subjectenzyme activity
dc.subjectenzyme assay
dc.subjectgenotype
dc.subjectimmunoprecipitation
dc.subjectmeiosis
dc.subjectmetaphase
dc.subjectnonhuman
dc.subjectnuclear localization
dc.subjectprotein localization
dc.subjectprotein modification
dc.subjectprotein phosphorylation
dc.subjectEukaryota
dc.subjectSaccharomycetales
dc.subjectBlotting, Western
dc.subjectCell Cycle Proteins
dc.subjectCell Nucleus
dc.subjectCyclin B
dc.subjectCyclin-Dependent Kinases
dc.subjectIntracellular Signaling Peptides and Proteins
dc.subjectMeiosis
dc.subjectMetaphase
dc.subjectPhosphorylation
dc.subjectProtein Tyrosine Phosphatases
dc.subjectProtein-Serine-Threonine Kinases
dc.subjectSaccharomyces cerevisiae
dc.subjectSaccharomyces cerevisiae Proteins
dc.subjectSignal Transduction
dc.typeArticle
dc.contributor.departmentBIOLOGICAL SCIENCES
dc.description.doi10.1371/journal.pone.0079001
dc.description.sourcetitlePLoS ONE
dc.description.volume8
dc.description.issue11
dc.description.pagee79001
dc.published.statePublished
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