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dc.contributor.authorMaekawa, Hiromi
dc.contributor.authorPriest, Claire
dc.contributor.authorLechner, Johannes
dc.contributor.authorPereira, Gislene
dc.contributor.authorSchiebel, Elmar
dc.date.accessioned2009-06-23T13:28:39Z
dc.date.available2009-06-23T13:28:39Z
dc.date.issued2007-11-05
dc.identifier.citationThe yeast centrosome translates the positional information of the anaphase spindle into a cell cycle signal. 2007, 179 (3):423-36 J. Cell Biol.en
dc.identifier.issn0021-9525
dc.identifier.pmid17967947
dc.identifier.doi10.1083/jcb.200705197
dc.identifier.urihttp://hdl.handle.net/10541/71278
dc.description.abstractThe spindle orientation checkpoint (SPOC) of budding yeast delays mitotic exit when cytoplasmic microtubules (MTs) are defective, causing the spindle to become misaligned. Delay is achieved by maintaining the activity of the Bfa1-Bub2 guanosine triphosphatase-activating protein complex, an inhibitor of mitotic exit. In this study, we show that the spindle pole body (SPB) component Spc72, a transforming acidic coiled coil-like molecule that interacts with the gamma-tubulin complex, recruits Kin4 kinase to both SPBs when cytoplasmic MTs are defective. This allows Kin4 to phosphorylate the SPB-associated Bfa1, rendering it resistant to inactivation by Cdc5 polo kinase. Consistently, forced targeting of Kin4 to both SPBs delays mitotic exit even when the anaphase spindle is correctly aligned. Moreover, we present evidence that Spc72 has an additional function in SPOC regulation that is independent of the recruitment of Kin4. Thus, Spc72 provides a missing link between cytoplasmic MT function and components of the SPOC.
dc.language.isoenen
dc.subject.meshAmino Acid Sequence
dc.subject.meshAnaphase
dc.subject.meshCell Cycle
dc.subject.meshCell Membrane
dc.subject.meshCentrosome
dc.subject.meshCytoskeletal Proteins
dc.subject.meshFungal Proteins
dc.subject.meshMicrotubule-Associated Proteins
dc.subject.meshMitotic Spindle Apparatus
dc.subject.meshModels, Biological
dc.subject.meshMolecular Sequence Data
dc.subject.meshPhosphorylation
dc.subject.meshProtein Kinases
dc.subject.meshSaccharomyces cerevisiae
dc.subject.meshSaccharomyces cerevisiae Proteins
dc.subject.meshSignal Transduction
dc.titleThe yeast centrosome translates the positional information of the anaphase spindle into a cell cycle signalen
dc.typeArticleen
dc.contributor.departmentZentrum für Molekulare Biologie and 2Biochemie-Zentrum, Universität Heidelberg, 69120 Heidelberg, Germany.en
dc.identifier.journalThe Journal of Cell Biologyen
html.description.abstractThe spindle orientation checkpoint (SPOC) of budding yeast delays mitotic exit when cytoplasmic microtubules (MTs) are defective, causing the spindle to become misaligned. Delay is achieved by maintaining the activity of the Bfa1-Bub2 guanosine triphosphatase-activating protein complex, an inhibitor of mitotic exit. In this study, we show that the spindle pole body (SPB) component Spc72, a transforming acidic coiled coil-like molecule that interacts with the gamma-tubulin complex, recruits Kin4 kinase to both SPBs when cytoplasmic MTs are defective. This allows Kin4 to phosphorylate the SPB-associated Bfa1, rendering it resistant to inactivation by Cdc5 polo kinase. Consistently, forced targeting of Kin4 to both SPBs delays mitotic exit even when the anaphase spindle is correctly aligned. Moreover, we present evidence that Spc72 has an additional function in SPOC regulation that is independent of the recruitment of Kin4. Thus, Spc72 provides a missing link between cytoplasmic MT function and components of the SPOC.


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