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dc.contributor.authorMaekawa, Hiromi
dc.contributor.authorSchiebel, Elmar
dc.date.accessioned2009-08-25T10:56:01Z
dc.date.available2009-08-25T10:56:01Z
dc.date.issued2004-07-15
dc.identifier.citationCdk1-Clb4 controls the interaction of astral microtubule plus ends with subdomains of the daughter cell cortex. 2004, 18 (14):1709-24 Genes Dev.en
dc.identifier.issn0890-9369
dc.identifier.pmid15256500
dc.identifier.doi10.1101/gad.298704
dc.identifier.urihttp://hdl.handle.net/10541/78435
dc.description.abstractAs in many polarized cells, spindle alignment in yeast is essential and cell cycle regulated. A key step that governs spindle alignment is the selective binding of the Kar9 protein to only one of the two spindle pole bodies (SPBs). It has been suggested that cyclin-dependent kinase Cdc28, in complex with cyclin Clb4, associates only with the SPB in the mother cell and so prevents Kar9 binding to this SPB. However, here we show that the nonoverexpressed Clb4 associates with the budward-directed SPB through Kar9. Cdc28-Clb4 then uses Kar9 as a carrier to move from this SPB to the plus ends of astral microtubules, where Cdc28-Clb4 regulates the interactions between microtubule ends and subdomains of the bud cortex. In the absence of Cdc28-Clb4 activity (G1/S phase), astral microtubules interact with the bud tip in a manner dependent on actin, Myo2, and Kar9. Coincidentally with reaching the bud cortex in S phase, Cdc28-Clb4 facilitates the dissociation of the microtubule bud tip interaction and their capture by the bud neck. This transition prevents the preanaphase spindle from becoming prematurely pulled into the bud. Thus, Cdc28-Clb4 facilitates spindle alignment by regulating the interaction of astral microtubules with subdomains of the bud cortex.
dc.language.isoenen
dc.subject.meshActins
dc.subject.meshCDC28 Protein Kinase, S cerevisiae
dc.subject.meshCell Polarity
dc.subject.meshCyclins
dc.subject.meshImmunoblotting
dc.subject.meshMicroscopy, Fluorescence
dc.subject.meshMicrotubules
dc.subject.meshMitotic Spindle Apparatus
dc.subject.meshMyosin Heavy Chains
dc.subject.meshMyosin Type V
dc.subject.meshNuclear Proteins
dc.subject.meshPlasmids
dc.subject.meshSaccharomyces cerevisiae
dc.subject.meshSaccharomyces cerevisiae Proteins
dc.titleCdk1-Clb4 controls the interaction of astral microtubule plus ends with subdomains of the daughter cell cortex.en
dc.typeArticle
dc.contributor.departmentThe Paterson Institute for Cancer Research, Christie Hospital NHS Trust, Wilmslow Road, Manchester M20 4BX, UK.en
dc.identifier.journalGenes & Developmenten
html.description.abstractAs in many polarized cells, spindle alignment in yeast is essential and cell cycle regulated. A key step that governs spindle alignment is the selective binding of the Kar9 protein to only one of the two spindle pole bodies (SPBs). It has been suggested that cyclin-dependent kinase Cdc28, in complex with cyclin Clb4, associates only with the SPB in the mother cell and so prevents Kar9 binding to this SPB. However, here we show that the nonoverexpressed Clb4 associates with the budward-directed SPB through Kar9. Cdc28-Clb4 then uses Kar9 as a carrier to move from this SPB to the plus ends of astral microtubules, where Cdc28-Clb4 regulates the interactions between microtubule ends and subdomains of the bud cortex. In the absence of Cdc28-Clb4 activity (G1/S phase), astral microtubules interact with the bud tip in a manner dependent on actin, Myo2, and Kar9. Coincidentally with reaching the bud cortex in S phase, Cdc28-Clb4 facilitates the dissociation of the microtubule bud tip interaction and their capture by the bud neck. This transition prevents the preanaphase spindle from becoming prematurely pulled into the bud. Thus, Cdc28-Clb4 facilitates spindle alignment by regulating the interaction of astral microtubules with subdomains of the bud cortex.


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