Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2001-7-19
pubmed:abstractText
The yeast Mps1p protein kinase acts in centrosome duplication and the spindle assembly checkpoint. We demonstrate here that a mouse Mps1p ortholog (esk, which we designate mMps1p) regulates centrosome duplication. Endogenous mMps1p and overexpressed GFP-mMps1p localize to centrosomes and kinetochores in mouse cells. Overexpression of GFP-mMps1p causes reduplication of centrosomes during S phase arrest. In contrast, a kinase-deficient mutant blocks centrosome duplication altogether. Control of centrosome duplication by mMps1p requires a known regulator of the process, Cdk2. Inhibition of Cdk2 prevents centrosome reduplication and destabilizes mMps1p, causing its subsequent loss from centrosomes, suggesting that Cdk2 promotes mMps1p's centrosome duplication function by regulating its stability during S phase. Thus, mMps1p, an in vitro Cdk2 substrate, regulates centrosome duplication jointly with Cdk2.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, http://linkedlifedata.com/resource/pubmed/chemical/CDC2-CDC28 Kinases, http://linkedlifedata.com/resource/pubmed/chemical/CDK2 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Cdk2 protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/Cell Cycle Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Cyclin-Dependent Kinase 2, http://linkedlifedata.com/resource/pubmed/chemical/Cyclin-Dependent Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Cysteine Endopeptidases, http://linkedlifedata.com/resource/pubmed/chemical/Green Fluorescent Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Luminescent Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Microtubule-Associated Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Multienzyme Complexes, http://linkedlifedata.com/resource/pubmed/chemical/Nocodazole, http://linkedlifedata.com/resource/pubmed/chemical/Proteasome Endopeptidase Complex, http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Protein-Tyrosine Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins, http://linkedlifedata.com/resource/pubmed/chemical/TTK protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Tetracycline, http://linkedlifedata.com/resource/pubmed/chemical/pericentrin
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0092-8674
pubmed:author
pubmed:issnType
Print
pubmed:day
13
pubmed:volume
106
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
95-104
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:11461705-3T3 Cells, pubmed-meshheading:11461705-Amino Acid Substitution, pubmed-meshheading:11461705-Animals, pubmed-meshheading:11461705-Antigens, pubmed-meshheading:11461705-CDC2-CDC28 Kinases, pubmed-meshheading:11461705-Cell Cycle, pubmed-meshheading:11461705-Cell Cycle Proteins, pubmed-meshheading:11461705-Centrosome, pubmed-meshheading:11461705-Cyclin-Dependent Kinase 2, pubmed-meshheading:11461705-Cyclin-Dependent Kinases, pubmed-meshheading:11461705-Cysteine Endopeptidases, pubmed-meshheading:11461705-Genes, Reporter, pubmed-meshheading:11461705-Green Fluorescent Proteins, pubmed-meshheading:11461705-Humans, pubmed-meshheading:11461705-Kinetochores, pubmed-meshheading:11461705-Luminescent Proteins, pubmed-meshheading:11461705-Mice, pubmed-meshheading:11461705-Microtubule-Associated Proteins, pubmed-meshheading:11461705-Mitosis, pubmed-meshheading:11461705-Multienzyme Complexes, pubmed-meshheading:11461705-Mutagenesis, Site-Directed, pubmed-meshheading:11461705-Nocodazole, pubmed-meshheading:11461705-Proteasome Endopeptidase Complex, pubmed-meshheading:11461705-Protein Kinases, pubmed-meshheading:11461705-Protein-Serine-Threonine Kinases, pubmed-meshheading:11461705-Protein-Tyrosine Kinases, pubmed-meshheading:11461705-Recombinant Fusion Proteins, pubmed-meshheading:11461705-S Phase, pubmed-meshheading:11461705-Telophase, pubmed-meshheading:11461705-Tetracycline, pubmed-meshheading:11461705-Transfection
pubmed:year
2001
pubmed:articleTitle
The mouse Mps1p-like kinase regulates centrosome duplication.
pubmed:affiliation
MCD Biology, UCB 347, University of Colorado, Boulder, Boulder, CO 80309, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't