Polo kinase links the stress pathway to cell cycle control and tip growth in fission yeast.

2.50
Hdl Handle:
http://hdl.handle.net/10541/74820
Title:
Polo kinase links the stress pathway to cell cycle control and tip growth in fission yeast.
Authors:
Petersen, Janni; Hagan, Iain M
Abstract:
Stress-activated mitogen-activated protein kinase cascades instigate a range of changes to enable eukaryotic cells to cope with particular insults. In Schizosaccharomyces pombe these responses include the transcription of specific gene sets and inhibition of entry into mitosis. The S. pombe stress response pathway (SRP) also promotes commitment to mitosis in unperturbed cell cycles to allow cells to match their rate of division with nutrient availability. The nature of this SRP function in cell cycle control is unknown. Entry into mitosis is controlled by mitosis-promoting factor (MPF; Cdc2/cyclin B) activity. Inhibitory phosphorylation of Cdc2 by Wee1 kinase inactivates MPF until Cdc25 removes this phosphate to promote mitosis. The balance between Wee1 and Cdc25 activities is influenced by the recruitment of polo kinase (Plo1) to the spindle pole body (SPB). The SPB component Cut12 mediates this recruitment. Hyper-activating mutations in either cut12 or plo1 enable Cdc25-defective cells to enter mitosis. The hyperactive cut12.s11 mutation suppresses cdc25.22, as it promotes recruitment of active Plo1 to interphase SPBs. Here we show that the SRP promotes phosphorylation of Plo1 on Ser 402. In unperturbed cell cycles, SRP-mediated phosphorylation of Ser 402 promotes Plo1 recruitment to SPBs and thus commitment to mitosis. Ser 402 phosphorylation also ensures efficient reinitiation of cell tip growth and cell division during recovery from particular stresses. Thus, phosphorylation of Plo1 Ser 402 not only enables SRP signalling to modulate the timing of mitotic commitment in response to nutrient status in unperturbed cycles, but also promotes the return to normal cell cycle control after stress.
Affiliation:
Cancer Research UK Cell Division Group, Paterson Institute for Cancer Research, Wilmslow Road, Manchester M20 4BX, UK.
Citation:
Polo kinase links the stress pathway to cell cycle control and tip growth in fission yeast. 2005, 435 (7041):507-12 Nature
Journal:
Nature
Issue Date:
26-May-2005
URI:
http://hdl.handle.net/10541/74820
DOI:
10.1038/nature03590
PubMed ID:
15917811
Type:
Article
Language:
en
ISSN:
1476-4687
Appears in Collections:
All Paterson Institute for Cancer Research

Full metadata record

DC FieldValue Language
dc.contributor.authorPetersen, Janni-
dc.contributor.authorHagan, Iain M-
dc.date.accessioned2009-07-21T16:50:47Z-
dc.date.available2009-07-21T16:50:47Z-
dc.date.issued2005-05-26-
dc.identifier.citationPolo kinase links the stress pathway to cell cycle control and tip growth in fission yeast. 2005, 435 (7041):507-12 Natureen
dc.identifier.issn1476-4687-
dc.identifier.pmid15917811-
dc.identifier.doi10.1038/nature03590-
dc.identifier.urihttp://hdl.handle.net/10541/74820-
dc.description.abstractStress-activated mitogen-activated protein kinase cascades instigate a range of changes to enable eukaryotic cells to cope with particular insults. In Schizosaccharomyces pombe these responses include the transcription of specific gene sets and inhibition of entry into mitosis. The S. pombe stress response pathway (SRP) also promotes commitment to mitosis in unperturbed cell cycles to allow cells to match their rate of division with nutrient availability. The nature of this SRP function in cell cycle control is unknown. Entry into mitosis is controlled by mitosis-promoting factor (MPF; Cdc2/cyclin B) activity. Inhibitory phosphorylation of Cdc2 by Wee1 kinase inactivates MPF until Cdc25 removes this phosphate to promote mitosis. The balance between Wee1 and Cdc25 activities is influenced by the recruitment of polo kinase (Plo1) to the spindle pole body (SPB). The SPB component Cut12 mediates this recruitment. Hyper-activating mutations in either cut12 or plo1 enable Cdc25-defective cells to enter mitosis. The hyperactive cut12.s11 mutation suppresses cdc25.22, as it promotes recruitment of active Plo1 to interphase SPBs. Here we show that the SRP promotes phosphorylation of Plo1 on Ser 402. In unperturbed cell cycles, SRP-mediated phosphorylation of Ser 402 promotes Plo1 recruitment to SPBs and thus commitment to mitosis. Ser 402 phosphorylation also ensures efficient reinitiation of cell tip growth and cell division during recovery from particular stresses. Thus, phosphorylation of Plo1 Ser 402 not only enables SRP signalling to modulate the timing of mitotic commitment in response to nutrient status in unperturbed cycles, but also promotes the return to normal cell cycle control after stress.en
dc.language.isoenen
dc.subject.meshCell Cycle-
dc.subject.meshCell Division-
dc.subject.meshMitogen-Activated Protein Kinases-
dc.subject.meshMitosis-
dc.subject.meshMitotic Spindle Apparatus-
dc.subject.meshMutation-
dc.subject.meshPhosphorylation-
dc.subject.meshPhosphoserine-
dc.subject.meshProtein-Serine-Threonine Kinases-
dc.subject.meshSchizosaccharomyces-
dc.subject.meshSchizosaccharomyces pombe Proteins-
dc.subject.meshSignal Transduction-
dc.subject.meshTemperature-
dc.titlePolo kinase links the stress pathway to cell cycle control and tip growth in fission yeast.en
dc.typeArticleen
dc.contributor.departmentCancer Research UK Cell Division Group, Paterson Institute for Cancer Research, Wilmslow Road, Manchester M20 4BX, UK.en
dc.identifier.journalNatureen

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