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dc.contributor.authorGrallert, Agnes
dc.contributor.authorChan, Kuan Yoow
dc.contributor.authorAlonso-Nunez, Maria-Luisa
dc.contributor.authorMadrid, Marisa
dc.contributor.authorBiswas, Ashapurna
dc.contributor.authorAlvarez-Tabares, Isabel
dc.contributor.authorConnolly, Yvonne
dc.contributor.authorTanaka, Kayoko
dc.contributor.authorRobertson, Alasdair M
dc.contributor.authorOrtiz, J
dc.contributor.authorSmith, Duncan L
dc.contributor.authorHagan, Iain M
dc.date.accessioned2013-03-15T16:29:50Z
dc.date.available2013-03-15T16:29:50Z
dc.date.issued2013-02-04
dc.identifier.citationRemoval of Centrosomal PP1 by NIMA Kinase Unlocks the MPF Feedback Loop to Promote Mitotic Commitment in S. pombe. 2013, 23 (3):213-22 Curr Biolen_GB
dc.identifier.issn1879-0445
dc.identifier.pmid23333317
dc.identifier.doi10.1016/j.cub.2012.12.039
dc.identifier.urihttp://hdl.handle.net/10541/273001
dc.description.abstractActivation of the Cdk1/cyclin B complex, also known as mitosis-promoting factor (MPF), drives commitment to mitosis. Interphase MPF is inhibited through phosphorylation of Cdk1 by Wee1-related kinases. Because Cdc25 phosphatases remove this phosphate, Cdc25 activity is an essential part of the switch that drives cells into mitosis. The generation of a critical "trigger" of active MPF promotes a positive feedback loop that employs Polo kinase to boost Cdc25 activity and inhibit Wee1, thereby ensuring that mitotic commitment is a bistable switch. Mutations in the spindle pole body (SPB) component Cut12 suppress otherwise lethal deficiencies in Cdc25.
dc.language.isoenen
dc.rightsArchived with thanks to Current biology : CBen_GB
dc.titleRemoval of Centrosomal PP1 by NIMA Kinase Unlocks the MPF Feedback Loop to Promote Mitotic Commitment in S. pombe.en
dc.typeArticleen
dc.contributor.departmentCRUK Cell Division Group, Paterson Institute for Cancer Research, University of Manchester, Wilmslow Road, Manchester M20 4BX, UK.en_GB
dc.identifier.journalCurrent Biologyen_GB
html.description.abstractActivation of the Cdk1/cyclin B complex, also known as mitosis-promoting factor (MPF), drives commitment to mitosis. Interphase MPF is inhibited through phosphorylation of Cdk1 by Wee1-related kinases. Because Cdc25 phosphatases remove this phosphate, Cdc25 activity is an essential part of the switch that drives cells into mitosis. The generation of a critical "trigger" of active MPF promotes a positive feedback loop that employs Polo kinase to boost Cdc25 activity and inhibit Wee1, thereby ensuring that mitotic commitment is a bistable switch. Mutations in the spindle pole body (SPB) component Cut12 suppress otherwise lethal deficiencies in Cdc25.


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