pubmed-article:18562292 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:18562292 | lifeskim:mentions | umls-concept:C0023689 | lld:lifeskim |
pubmed-article:18562292 | lifeskim:mentions | umls-concept:C0041538 | lld:lifeskim |
pubmed-article:18562292 | lifeskim:mentions | umls-concept:C0694888 | lld:lifeskim |
pubmed-article:18562292 | lifeskim:mentions | umls-concept:C1417659 | lld:lifeskim |
pubmed-article:18562292 | lifeskim:mentions | umls-concept:C0475264 | lld:lifeskim |
pubmed-article:18562292 | lifeskim:mentions | umls-concept:C0205360 | lld:lifeskim |
pubmed-article:18562292 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
pubmed-article:18562292 | pubmed:issue | 25 | lld:pubmed |
pubmed-article:18562292 | pubmed:dateCreated | 2008-6-25 | lld:pubmed |
pubmed-article:18562292 | pubmed:abstractText | PTEN is a tumor suppressor frequently mutated in cancer. Recent reports implicated Nedd4-1 as the E3 ubiquitin ligase for PTEN that regulates its stability and nuclear localization. We tested the physiological role of Nedd4-1 as a PTEN regulator by using cells and tissues derived from two independently generated strains of mice with their Nedd4-1 gene disrupted. PTEN stability and ubiquitination were indistinguishable between the wild-type and Nedd4-1-deficient cells, and an interaction between the two proteins could not be detected. Moreover, PTEN subcellular distribution, showing prominent cytoplasmic and nuclear staining, was independent of Nedd4-1 presence. Finally, activation of PKB/Akt, a major downstream target of cytoplasmic PTEN activity, and the ability of PTEN to transactivate the Rad51 promoter, a measure of its nuclear function, were unaffected by the loss of Nedd4-1. Taken together, our results fail to support a role for Nedd4-1 as the E3 ligase regulating PTEN stability and subcellular localization. | lld:pubmed |
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pubmed-article:18562292 | pubmed:language | eng | lld:pubmed |
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pubmed-article:18562292 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:18562292 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:18562292 | pubmed:month | Jun | lld:pubmed |
pubmed-article:18562292 | pubmed:issn | 1091-6490 | lld:pubmed |
pubmed-article:18562292 | pubmed:author | pubmed-author:RotinDanielaD | lld:pubmed |
pubmed-article:18562292 | pubmed:author | pubmed-author:BroseNilsN | lld:pubmed |
pubmed-article:18562292 | pubmed:author | pubmed-author:ChenLuL | lld:pubmed |
pubmed-article:18562292 | pubmed:author | pubmed-author:KawabeHiroshi... | lld:pubmed |
pubmed-article:18562292 | pubmed:author | pubmed-author:StambolicVukV | lld:pubmed |
pubmed-article:18562292 | pubmed:author | pubmed-author:FouladkouFate... | lld:pubmed |
pubmed-article:18562292 | pubmed:author | pubmed-author:NeebAntjeA | lld:pubmed |
pubmed-article:18562292 | pubmed:author | pubmed-author:LandryTamaraT | lld:pubmed |
pubmed-article:18562292 | pubmed:issnType | Electronic | lld:pubmed |
pubmed-article:18562292 | pubmed:day | 24 | lld:pubmed |
pubmed-article:18562292 | pubmed:volume | 105 | lld:pubmed |
pubmed-article:18562292 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:18562292 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:18562292 | pubmed:pagination | 8585-90 | lld:pubmed |
pubmed-article:18562292 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
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pubmed-article:18562292 | pubmed:year | 2008 | lld:pubmed |
pubmed-article:18562292 | pubmed:articleTitle | The ubiquitin ligase Nedd4-1 is dispensable for the regulation of PTEN stability and localization. | lld:pubmed |
pubmed-article:18562292 | pubmed:affiliation | Hospital for Sick Children and Biochemistry Department, University of Toronto, MaRS-TMDT, 101 College Street, Toronto, Ontario M5G 1L7, Canada. | lld:pubmed |
pubmed-article:18562292 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:18562292 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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