Source:http://linkedlifedata.com/resource/pubmed/id/15107609
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
5
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pubmed:dateCreated |
2004-5-21
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pubmed:abstractText |
The mitosis promoting phosphatase, cdc25C, is a target of both the DNA replication and DNA damage checkpoint pathways. These pathways regulate cdc25C function, in part, by promoting the association of cdc25C with 14-3-3 proteins, which results in the retention of cdc25C in the cytoplasm. To determine which 14-3-3 proteins were required to regulate cdc25C function, we tested the ability of various 14-3-3 family members to form a complex with and negatively regulate cdc25C in human cells. Two 14-3-3 family members, 14-3-3epsilon and 14-3-3gamma specifically formed a complex with cdc25C but not with the 14-3-3 binding defective cdc25C mutant, S216A. In addition, 14-3-3epsilon and 14-3-3gamma inhibited the ability of cdc25C, but not the S216A mutant, to induce premature chromatin condensation (PCC) in U-2OS cells. These results suggested that the reduction in PCC by 14-3-3epsilon and 14-3-3gamma was due to inhibition of cdc25C function. In contrast, 14-3-3sigma was unable to form a complex with cdc25C, but was able to inhibit the ability of both wild type cdc25C and S216A to induce PCC. This suggests that 14-3-3sigma regulates entry into mitosis independently of cdc25C and 14-3-3epsilon and 14-3-3gamma. Thus, specific members of the 14-3-3 family of proteins may act coordinately to maintain the DNA replication checkpoint by regulating the activity of different cell cycle proteins.
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pubmed:language |
eng
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pubmed:journal | |
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/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Isoforms,
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 |
May
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pubmed:issn |
1538-4101
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
3
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
672-7
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:15107609-14-3-3 Proteins,
pubmed-meshheading:15107609-Animals,
pubmed-meshheading:15107609-Cell Cycle Proteins,
pubmed-meshheading:15107609-Cell Line, Tumor,
pubmed-meshheading:15107609-Cell Nucleus,
pubmed-meshheading:15107609-Humans,
pubmed-meshheading:15107609-Macromolecular Substances,
pubmed-meshheading:15107609-Mitosis,
pubmed-meshheading:15107609-Multigene Family,
pubmed-meshheading:15107609-Phylogeny,
pubmed-meshheading:15107609-Protein Binding,
pubmed-meshheading:15107609-Protein Isoforms,
pubmed-meshheading:15107609-Recombinant Fusion Proteins,
pubmed-meshheading:15107609-Tyrosine 3-Monooxygenase,
pubmed-meshheading:15107609-cdc25 Phosphatases
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pubmed:year |
2004
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pubmed:articleTitle |
14-3-3 family members act coordinately to regulate mitotic progression.
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pubmed:affiliation |
Department of Adult Oncology, Dana Farber Cancer Institute and Harvard Medical School, Boston, Massachusetts 02115, USA. sdalal@@actrec.res.in
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pubmed:publicationType |
Journal Article
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