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http://purl.uniprot.org/citations/17290220http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17290220http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17290220http://www.w3.org/2000/01/rdf-schema#comment"Mdm2 is an E3 ubiquitin ligase that promotes its own ubiquitination and also ubiquitination of the p53 tumour suppressor. In a bacterial two-hybrid screen, using Mdm2 as bait, we identified an Mdm2-interacting peptide that bears sequence similarity to the deubiquitinating enzyme USP2a. We have established that full-length USP2a associates with Mdm2 in cells where it can deubiquitinate Mdm2 while demonstrating no deubiquitinating activity towards p53. Ectopic expression of USP2a causes accumulation of Mdm2 in a dose-dependent manner and consequently promotes Mdm2-mediated p53 degradation. This differs from the behaviour of HAUSP, which deubiquitinates p53 in addition to Mdm2 and thus protects p53 from Mdm2-mediated degradation. We further demonstrate that suppression of endogenous USP2a destabilises Mdm2 and causes accumulation of p53 protein and activation of p53. Our data identify the deubiquitinating enzyme USP2a as a novel regulator of the p53 pathway that acts through its ability to selectively target Mdm2."xsd:string
http://purl.uniprot.org/citations/17290220http://purl.org/dc/terms/identifier"doi:10.1038/sj.emboj.7601567"xsd:string
http://purl.uniprot.org/citations/17290220http://purl.org/dc/terms/identifier"doi:10.1038/sj.emboj.7601567"xsd:string
http://purl.uniprot.org/citations/17290220http://purl.uniprot.org/core/author"Lane D.P."xsd:string
http://purl.uniprot.org/citations/17290220http://purl.uniprot.org/core/author"Lane D.P."xsd:string
http://purl.uniprot.org/citations/17290220http://purl.uniprot.org/core/author"Stevenson L.F."xsd:string
http://purl.uniprot.org/citations/17290220http://purl.uniprot.org/core/author"Stevenson L.F."xsd:string
http://purl.uniprot.org/citations/17290220http://purl.uniprot.org/core/author"Allende-Vega N."xsd:string
http://purl.uniprot.org/citations/17290220http://purl.uniprot.org/core/author"Allende-Vega N."xsd:string
http://purl.uniprot.org/citations/17290220http://purl.uniprot.org/core/author"Saville M.K."xsd:string
http://purl.uniprot.org/citations/17290220http://purl.uniprot.org/core/author"Saville M.K."xsd:string
http://purl.uniprot.org/citations/17290220http://purl.uniprot.org/core/author"Sparks A."xsd:string
http://purl.uniprot.org/citations/17290220http://purl.uniprot.org/core/author"Sparks A."xsd:string
http://purl.uniprot.org/citations/17290220http://purl.uniprot.org/core/author"Xirodimas D.P."xsd:string
http://purl.uniprot.org/citations/17290220http://purl.uniprot.org/core/author"Xirodimas D.P."xsd:string
http://purl.uniprot.org/citations/17290220http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17290220http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17290220http://purl.uniprot.org/core/name"EMBO J."xsd:string
http://purl.uniprot.org/citations/17290220http://purl.uniprot.org/core/name"EMBO J."xsd:string
http://purl.uniprot.org/citations/17290220http://purl.uniprot.org/core/pages"976-986"xsd:string
http://purl.uniprot.org/citations/17290220http://purl.uniprot.org/core/pages"976-986"xsd:string
http://purl.uniprot.org/citations/17290220http://purl.uniprot.org/core/title"The deubiquitinating enzyme USP2a regulates the p53 pathway by targeting Mdm2."xsd:string
http://purl.uniprot.org/citations/17290220http://purl.uniprot.org/core/title"The deubiquitinating enzyme USP2a regulates the p53 pathway by targeting Mdm2."xsd:string