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rdf:type |
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lifeskim:mentions |
umls-concept:C0079419,
umls-concept:C0205263,
umls-concept:C0205314,
umls-concept:C0243125,
umls-concept:C0679622,
umls-concept:C0699900,
umls-concept:C0812222,
umls-concept:C1414625,
umls-concept:C1704259,
umls-concept:C1704735,
umls-concept:C1705987,
umls-concept:C1879547
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pubmed:issue |
4
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pubmed:dateCreated |
2009-2-23
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pubmed:abstractText |
The p53 tumour suppressor protein is tightly controlled by the E3 ubiquitin ligase, mouse double minute 2 (MDM2), but maintains MDM2 expression as part of a negative feedback loop. We have identified the immunophilin, 25kDa FK506-binding protein (FKBP25), previously shown to be regulated by p53-mediated repression, as an MDM2-interacting partner. We show that FKBP25 stimulates auto-ubiquitylation and proteasomal degradation of MDM2, leading to the induction of p53. Depletion of FKBP25 by siRNA leads to increased levels of MDM2 and a corresponding reduction in p53 and p21 levels. These data are consistent with the idea that FKBP25 contributes to regulation of the p53-MDM2 negative feedback loop.
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pubmed:grant |
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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/Cyclin-Dependent Kinase Inhibitor...,
http://linkedlifedata.com/resource/pubmed/chemical/FKBP3 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Glutathione Transferase,
http://linkedlifedata.com/resource/pubmed/chemical/Luciferases,
http://linkedlifedata.com/resource/pubmed/chemical/MDM2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Proteasome Endopeptidase Complex,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-mdm2,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Small Interfering,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Tacrolimus Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Tumor Suppressor Protein p53,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitin-Protein Ligases
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
1873-3468
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
18
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pubmed:volume |
583
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
621-6
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pubmed:meshHeading |
pubmed-meshheading:19166840-Animals,
pubmed-meshheading:19166840-Cell Line, Tumor,
pubmed-meshheading:19166840-Cyclin-Dependent Kinase Inhibitor p21,
pubmed-meshheading:19166840-Escherichia coli,
pubmed-meshheading:19166840-Gene Expression Regulation, Neoplastic,
pubmed-meshheading:19166840-Genes, Reporter,
pubmed-meshheading:19166840-Glutathione Transferase,
pubmed-meshheading:19166840-HCT116 Cells,
pubmed-meshheading:19166840-Humans,
pubmed-meshheading:19166840-Luciferases,
pubmed-meshheading:19166840-Mice,
pubmed-meshheading:19166840-Proteasome Endopeptidase Complex,
pubmed-meshheading:19166840-Proto-Oncogene Proteins c-mdm2,
pubmed-meshheading:19166840-RNA, Small Interfering,
pubmed-meshheading:19166840-Recombinant Fusion Proteins,
pubmed-meshheading:19166840-Tacrolimus Binding Proteins,
pubmed-meshheading:19166840-Transfection,
pubmed-meshheading:19166840-Tumor Suppressor Protein p53,
pubmed-meshheading:19166840-Ubiquitin-Protein Ligases,
pubmed-meshheading:19166840-Ubiquitination
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pubmed:year |
2009
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pubmed:articleTitle |
FKBP25, a novel regulator of the p53 pathway, induces the degradation of MDM2 and activation of p53.
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pubmed:affiliation |
Biomedical Research Institute, Ninewells Hospital and Medical School, University of Dundee, Level 5, University of Dundee, Dundee DD1 9SY, United Kingdom.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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