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dc.contributor.authorGrallert, Agnes
dc.contributor.authorHagan, Iain M
dc.date.accessioned2009-10-05T15:51:44Z
dc.date.available2009-10-05T15:51:44Z
dc.date.issued2002-06-17
dc.identifier.citationSchizosaccharomyces pombe NIMA-related kinase, Fin1, regulates spindle formation and an affinity of Polo for the SPB. 2002, 21 (12):3096-107 EMBO J.en
dc.identifier.issn0261-4189
dc.identifier.pmid12065422
dc.identifier.doi10.1093/emboj/cdf294
dc.identifier.urihttp://hdl.handle.net/10541/83550
dc.description.abstractThe Aspergillus nidulans protein kinase NIMA regulates mitotic commitment, while the human and Xenopus equivalents influence centrosome function. Two recessive, temperature-sensitive mutations in the Schizosaccharomyces pombe NIMA homologue, Fin1, blocked spindle formation at 37 degrees C. One of the two spindle pole bodies (SPBs) failed to nucleate microtubules. This phenotype was reduced by accelerating mitotic commitment through genetic inhibition of Wee1 or activation of either Cdc25 or Cdc2. Polo kinase (Plo1) normally associates with the SPB of mitotic, but not interphase cells. cut12.s11 is a dominant mutation in an SPB component that both suppresses cdc25 mutants and promotes Plo1 association with the interphase SPB. Both cut12.s11 phenotypes were abolished by removing Fin1 function. Elevating Fin1 levels promoted Plo1 recruitment to the interphase SPB of wild-type cells and reduced the severity of the cdc25.22 phenotype. These data are consistent with Fin1 regulating Plo1 function during mitotic commitment. The fin1 mitotic commitment and spindle phenotypes resemble distinct nimA phenotypes in different systems and suggest that the function of this family of kinases may be conserved across species.
dc.language.isoenen
dc.subject.meshAnimals
dc.subject.meshCell Cycle
dc.subject.meshCell Cycle Proteins
dc.subject.meshDrosophila Proteins
dc.subject.meshHumans
dc.subject.meshMicrotubule-Associated Proteins
dc.subject.meshMitotic Spindle Apparatus
dc.subject.meshModels, Biological
dc.subject.meshNuclear Proteins
dc.subject.meshPhosphoproteins
dc.subject.meshProtein-Serine-Threonine Kinases
dc.subject.meshRecombinant Fusion Proteins
dc.subject.meshSchizosaccharomyces
dc.subject.meshSchizosaccharomyces pombe Proteins
dc.titleSchizosaccharomyces pombe NIMA-related kinase, Fin1, regulates spindle formation and an affinity of Polo for the SPB.en
dc.typeArticleen
dc.contributor.departmentPaterson Institute for Cancer Research, Wilmslow Road, Manchester M20 4BX, UK.en
dc.identifier.journalThe EMBO Journalen
html.description.abstractThe Aspergillus nidulans protein kinase NIMA regulates mitotic commitment, while the human and Xenopus equivalents influence centrosome function. Two recessive, temperature-sensitive mutations in the Schizosaccharomyces pombe NIMA homologue, Fin1, blocked spindle formation at 37 degrees C. One of the two spindle pole bodies (SPBs) failed to nucleate microtubules. This phenotype was reduced by accelerating mitotic commitment through genetic inhibition of Wee1 or activation of either Cdc25 or Cdc2. Polo kinase (Plo1) normally associates with the SPB of mitotic, but not interphase cells. cut12.s11 is a dominant mutation in an SPB component that both suppresses cdc25 mutants and promotes Plo1 association with the interphase SPB. Both cut12.s11 phenotypes were abolished by removing Fin1 function. Elevating Fin1 levels promoted Plo1 recruitment to the interphase SPB of wild-type cells and reduced the severity of the cdc25.22 phenotype. These data are consistent with Fin1 regulating Plo1 function during mitotic commitment. The fin1 mitotic commitment and spindle phenotypes resemble distinct nimA phenotypes in different systems and suggest that the function of this family of kinases may be conserved across species.


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