Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
32
pubmed:dateCreated
2005-8-8
pubmed:abstractText
Budding and fission yeast Cdc14 homologues, a conserved family of serine-threonine phosphatases, play a role in the inactivation of mitotic cyclin-dependent kinases (CDKs) by molecularly distinct mechanisms. Saccharomyces cerevisiae Cdc14 protein phosphatase inactivates CDKs by promoting mitotic cyclin degradation and the accumulation of a CDK inhibitor to allow budding yeast cells to exit from mitosis. Schizosaccharomyces pombe Flp1 phosphatase down-regulates CDK/cyclin activity, controlling the degradation of the Cdc25 tyrosine phosphatase for fission yeast cells to undergo cytokinesis. In the present work, we show that human Cdc14 homologues (hCdc14A and hCdc14B) rescued flp1-deficient fission yeast strains, indicating functional homology. We also show that hCdc14A and B interacted in vivo with S. pombe Cdc25 and that hCdc14A dephosphorylated this mitotic inducer both in vitro and in vivo. Our results support a Cdc14 conserved inhibitory mechanism acting on S. pombe Cdc25 protein and suggest that human cells may regulate Cdc25 in a similar manner to inactivate Cdk1-mitotic cyclin complexes.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/CDC14 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/CDC14 protein, S pombe, http://linkedlifedata.com/resource/pubmed/chemical/CDC14A protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Cell Cycle Proteins, http://linkedlifedata.com/resource/pubmed/chemical/DNA, http://linkedlifedata.com/resource/pubmed/chemical/FLP1 protein, S pombe, http://linkedlifedata.com/resource/pubmed/chemical/Glutathione Transferase, http://linkedlifedata.com/resource/pubmed/chemical/Phosphoprotein Phosphatases, http://linkedlifedata.com/resource/pubmed/chemical/Phosphoric Monoester Hydrolases, http://linkedlifedata.com/resource/pubmed/chemical/Protein Tyrosine Phosphatases, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Schizosaccharomyces pombe Proteins
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
12
pubmed:volume
280
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
29144-50
pubmed:dateRevised
2008-10-29
pubmed:meshHeading
pubmed-meshheading:15911625-Blotting, Western, pubmed-meshheading:15911625-Cell Cycle Proteins, pubmed-meshheading:15911625-Cell Nucleus, pubmed-meshheading:15911625-Cytokinesis, pubmed-meshheading:15911625-DNA, pubmed-meshheading:15911625-Down-Regulation, pubmed-meshheading:15911625-Flow Cytometry, pubmed-meshheading:15911625-Genetic Complementation Test, pubmed-meshheading:15911625-Glutathione Transferase, pubmed-meshheading:15911625-Humans, pubmed-meshheading:15911625-Immunoprecipitation, pubmed-meshheading:15911625-Microscopy, Fluorescence, pubmed-meshheading:15911625-Mitosis, pubmed-meshheading:15911625-Mitotic Spindle Apparatus, pubmed-meshheading:15911625-Phenotype, pubmed-meshheading:15911625-Phosphoprotein Phosphatases, pubmed-meshheading:15911625-Phosphoric Monoester Hydrolases, pubmed-meshheading:15911625-Phosphorylation, pubmed-meshheading:15911625-Plasmids, pubmed-meshheading:15911625-Protein Binding, pubmed-meshheading:15911625-Protein Tyrosine Phosphatases, pubmed-meshheading:15911625-Recombinant Fusion Proteins, pubmed-meshheading:15911625-Saccharomyces cerevisiae Proteins, pubmed-meshheading:15911625-Schizosaccharomyces, pubmed-meshheading:15911625-Schizosaccharomyces pombe Proteins, pubmed-meshheading:15911625-Temperature
pubmed:year
2005
pubmed:articleTitle
Functional homology among human and fission yeast Cdc14 phosphatases.
pubmed:affiliation
Centro de Investigación del Cáncer and Departamento de Microbiología y Genética, Campus Miguel de Unamuno, Universidad de Salamanca/Consejo Superior de Investigaciones Científicas, 37007 Salamanca, Spain.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't