Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
23
pubmed:dateCreated
2008-12-23
pubmed:abstractText
In eukaryotic cells, fidelity in transmission of genetic information during cell division is ensured by the action of cell cycle checkpoints. Checkpoints are surveillance mechanisms that arrest or delay cell cycle progression when critical cellular processes are defective or when the genome is damaged. During meiosis, the so-called meiotic recombination checkpoint blocks entry into meiosis I until recombination has been completed, thus avoiding aberrant chromosome segregation and the formation of aneuploid gametes. One of the key components of the meiotic recombination checkpoint is the meiosis-specific Mek1 kinase, which belongs to the family of Rad53/Cds1/Chk2 checkpoint kinases containing forkhead-associated domains. In fission yeast, several lines of evidence suggest that Mek1 targets the critical cell cycle regulator Cdc25 to delay meiotic cell cycle progression. Here, we investigate in more detail the molecular mechanism of action of the fission yeast Mek1 protein. We demonstrate that Mek1 acts independently of Cds1 to phosphorylate Cdc25, and this phosphorylation is required to trigger cell cycle arrest. Using ectopic overexpression of mek1(+) as a tool to induce in vivo activation of Mek1, we find that Mek1 promotes cytoplasmic accumulation of Cdc25 and results in prolonged phosphorylation of Cdc2 at tyrosine 15. We propose that at least one of the mechanisms contributing to the cell cycle delay when the meiotic recombination checkpoint is activated in fission yeast is the nuclear exclusion of the Cdc25 phosphatase by Mek1-dependent phosphorylation.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/14-3-3 Proteins, http://linkedlifedata.com/resource/pubmed/chemical/CDC2 Protein Kinase, http://linkedlifedata.com/resource/pubmed/chemical/Cell Cycle Proteins, http://linkedlifedata.com/resource/pubmed/chemical/DNA, Fungal, http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Intracellular Signaling Peptides..., http://linkedlifedata.com/resource/pubmed/chemical/MAP Kinase Kinase 1, http://linkedlifedata.com/resource/pubmed/chemical/Mek1 protein, S pombe, http://linkedlifedata.com/resource/pubmed/chemical/Phosphotyrosine, http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Schizosaccharomyces pombe Proteins, http://linkedlifedata.com/resource/pubmed/chemical/cdc2 protein, S pombe, http://linkedlifedata.com/resource/pubmed/chemical/checkpoint kinase 2, http://linkedlifedata.com/resource/pubmed/chemical/rad24 protein, S pombe, http://linkedlifedata.com/resource/pubmed/chemical/ras-GRF1
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
1551-4005
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
7
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3720-30
pubmed:dateRevised
2011-11-2
pubmed:meshHeading
pubmed-meshheading:19029820-14-3-3 Proteins, pubmed-meshheading:19029820-CDC2 Protein Kinase, pubmed-meshheading:19029820-Cell Cycle Proteins, pubmed-meshheading:19029820-Cell Nucleus, pubmed-meshheading:19029820-DNA, Fungal, pubmed-meshheading:19029820-DNA Replication, pubmed-meshheading:19029820-Fungal Proteins, pubmed-meshheading:19029820-Intracellular Signaling Peptides and Proteins, pubmed-meshheading:19029820-MAP Kinase Kinase 1, pubmed-meshheading:19029820-Meiosis, pubmed-meshheading:19029820-Phosphorylation, pubmed-meshheading:19029820-Phosphotyrosine, pubmed-meshheading:19029820-Protein Transport, pubmed-meshheading:19029820-Protein-Serine-Threonine Kinases, pubmed-meshheading:19029820-Schizosaccharomyces, pubmed-meshheading:19029820-Schizosaccharomyces pombe Proteins, pubmed-meshheading:19029820-ras-GRF1
pubmed:year
2008
pubmed:articleTitle
The fission yeast meiotic checkpoint kinase Mek1 regulates nuclear localization of Cdc25 by phosphorylation.
pubmed:affiliation
Instituto de Biología Molecular y Celular del Cáncer, Consejo Superior de Investigaciones Científicas and Universidad de Salamanca, Salamanca, Spain.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't