Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2003-2-17
pubmed:abstractText
Mkp1 ( MAPKAP kinase Schizosaccharomyces pombe 1) and Mkp2 are two members from fission yeast of the sub-class of putative MAPK-activated protein kinases in yeasts, the other known members being Rck1 and Rck2 from Saccharomyces cerevisiae. The Mkp1 protein is readily co-immunoprecipitated with Sty1 from S. pombe extracts; Mkp2 shows a weaker interaction with Sty1. In mkp1 mutants, conjugation and meiosis proceed more readily and rapidly than in wild-type cells, in analogy to what was previously found for S. cerevisiae rck1 mutants. Conversely, overexpression of mkp1(+) delays meiosis. Mkp1 is phosphorylated in vivo in a sty1(+)-dependent manner; this modification is removed when cells are starved for nitrogen, a condition that is conducive to entry into stationary phase and meiosis. Overexpression of mkp1(+), like a sty1 mutation, also causes vegetative cells to elongate. The level of Mkp1 phosphorylation drops as cells enter mitosis. We have localised Mkp1 to the cytoplasm, excluded from the nucleus, in vegetative cells. The Mkp1 protein accumulates in zygotic asci and is concentrated within spores. The mkp2(+) gene has no noticeable impact on meiosis. Mkp2 is excluded from the nucleus in vegetative cells, and is concentrated at the septa of dividing cells. Mkp2 does not accumulate in meiotic cells.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
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-activated kinase 2, http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Nitrogen, http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases, http://linkedlifedata.com/resource/pubmed/chemical/RCK1 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/RCK2 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/SRK1 protein, S pombe, http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Schizosaccharomyces pombe Proteins, http://linkedlifedata.com/resource/pubmed/chemical/sty1 protein, S pombe
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
1617-4615
pubmed:author
pubmed:issnType
Print
pubmed:volume
268
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
585-97
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:12589433-Amino Acid Sequence, pubmed-meshheading:12589433-Conjugation, Genetic, pubmed-meshheading:12589433-Fungal Proteins, pubmed-meshheading:12589433-Genes, Fungal, pubmed-meshheading:12589433-Intracellular Signaling Peptides and Proteins, pubmed-meshheading:12589433-Meiosis, pubmed-meshheading:12589433-Mitogen-Activated Protein Kinases, pubmed-meshheading:12589433-Mitosis, pubmed-meshheading:12589433-Models, Biological, pubmed-meshheading:12589433-Molecular Sequence Data, pubmed-meshheading:12589433-Mutation, pubmed-meshheading:12589433-Nitrogen, pubmed-meshheading:12589433-Phosphorylation, pubmed-meshheading:12589433-Protein-Serine-Threonine Kinases, pubmed-meshheading:12589433-Saccharomyces cerevisiae, pubmed-meshheading:12589433-Saccharomyces cerevisiae Proteins, pubmed-meshheading:12589433-Schizosaccharomyces, pubmed-meshheading:12589433-Schizosaccharomyces pombe Proteins, pubmed-meshheading:12589433-Sequence Homology, Amino Acid, pubmed-meshheading:12589433-Species Specificity
pubmed:year
2003
pubmed:articleTitle
Mkp1 and Mkp2, two MAPKAP-kinase homologues in Schizosaccharomyces pombe, interact with the MAP kinase Sty1.
pubmed:affiliation
Department of Cell and Molecular Biology, Lundberg Laboratory, Göteborg University, P.O. Box 462, 405 30, Göteborg, Sweden.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't