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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5331
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pubmed:dateCreated |
1997-9-22
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pubmed:abstractText |
Human Cdc25C is a dual-specificity protein phosphatase that controls entry into mitosis by dephosphorylating the protein kinase Cdc2. Throughout interphase, but not in mitosis, Cdc25C was phosphorylated on serine-216 and bound to members of the highly conserved and ubiquitously expressed family of 14-3-3 proteins. A mutation preventing phosphorylation of serine-216 abrogated 14-3-3 binding. Conditional overexpression of this mutant perturbed mitotic timing and allowed cells to escape the G2 checkpoint arrest induced by either unreplicated DNA or radiation-induced damage. Chk1, a fission yeast kinase involved in the DNA damage checkpoint response, phosphorylated Cdc25C in vitro on serine-216. These results indicate that serine-216 phosphorylation and 14-3-3 binding negatively regulate Cdc25C and identify Cdc25C as a potential target of checkpoint control in human cells.
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pubmed:grant |
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pubmed:commentsCorrections |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/14-3-3 Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/CDC25C protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Cell Cycle Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Checkpoint kinase 1,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoserine,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Tyrosine 3-Monooxygenase,
http://linkedlifedata.com/resource/pubmed/chemical/cdc25 Phosphatases
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0036-8075
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
5
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pubmed:volume |
277
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1501-5
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pubmed:dateRevised |
2011-11-2
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pubmed:meshHeading |
pubmed-meshheading:9278512-14-3-3 Proteins,
pubmed-meshheading:9278512-Amino Acid Sequence,
pubmed-meshheading:9278512-Cell Cycle Proteins,
pubmed-meshheading:9278512-DNA Damage,
pubmed-meshheading:9278512-DNA Replication,
pubmed-meshheading:9278512-G2 Phase,
pubmed-meshheading:9278512-Gamma Rays,
pubmed-meshheading:9278512-HeLa Cells,
pubmed-meshheading:9278512-Humans,
pubmed-meshheading:9278512-Jurkat Cells,
pubmed-meshheading:9278512-Mitosis,
pubmed-meshheading:9278512-Molecular Sequence Data,
pubmed-meshheading:9278512-Mutation,
pubmed-meshheading:9278512-Phosphorylation,
pubmed-meshheading:9278512-Phosphoserine,
pubmed-meshheading:9278512-Protein Kinases,
pubmed-meshheading:9278512-Proteins,
pubmed-meshheading:9278512-Recombinant Fusion Proteins,
pubmed-meshheading:9278512-S Phase,
pubmed-meshheading:9278512-Tyrosine 3-Monooxygenase,
pubmed-meshheading:9278512-cdc25 Phosphatases
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pubmed:year |
1997
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pubmed:articleTitle |
Mitotic and G2 checkpoint control: regulation of 14-3-3 protein binding by phosphorylation of Cdc25C on serine-216.
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pubmed:affiliation |
Department of Cell Biology and Physiology, Washington University School of Medicine, 660 South Euclid Avenue, St. Louis, MO 63110, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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