pubmed-article:15355975 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:15355975 | lifeskim:mentions | umls-concept:C0079427 | lld:lifeskim |
pubmed-article:15355975 | lifeskim:mentions | umls-concept:C0031715 | lld:lifeskim |
pubmed-article:15355975 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
pubmed-article:15355975 | lifeskim:mentions | umls-concept:C0694888 | lld:lifeskim |
pubmed-article:15355975 | lifeskim:mentions | umls-concept:C1325410 | lld:lifeskim |
pubmed-article:15355975 | lifeskim:mentions | umls-concept:C0205360 | lld:lifeskim |
pubmed-article:15355975 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
pubmed-article:15355975 | pubmed:issue | 44 | lld:pubmed |
pubmed-article:15355975 | pubmed:dateCreated | 2004-10-25 | lld:pubmed |
pubmed-article:15355975 | pubmed:abstractText | The tumor suppressor PTEN plays an essential role in regulating signaling pathways involved in cell growth and apoptosis and is inactivated in a wide variety of tumors. In this study, we have identified a protein, referred to as PICT-1 (protein interacting with carboxyl terminus 1), that binds to the C terminus of PTEN and regulates its phosphorylation and turnover. Down-regulation of PICT-1 in MCF7 cells by RNA interference enhances the degradation of PTEN with a concomitant decrease in its phosphorylation. PTEN C-terminal tumor-associated mutants, which are highly susceptible to protein degradation, have lost the ability to bind to PICT-1 along with their reduced phosphorylation, suggesting that their rapid turnover results from impaired binding to PICT-1. Our results identify PICT-1 as a PTEN-interacting protein that promotes the phosphorylation and stability of PTEN. These findings suggest a novel molecular mechanism underlying the turnover of PTEN, which also provides an explanation for the loss of PTEN function due to C-terminal mutations. | lld:pubmed |
pubmed-article:15355975 | pubmed:language | eng | lld:pubmed |
pubmed-article:15355975 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15355975 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:15355975 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15355975 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:15355975 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15355975 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:15355975 | pubmed:month | Oct | lld:pubmed |
pubmed-article:15355975 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:15355975 | pubmed:author | pubmed-author:KanahoYasunor... | lld:pubmed |
pubmed-article:15355975 | pubmed:author | pubmed-author:MaehamaTomohi... | lld:pubmed |
pubmed-article:15355975 | pubmed:author | pubmed-author:IkawaHidekiH | lld:pubmed |
pubmed-article:15355975 | pubmed:author | pubmed-author:OkaharaFumiak... | lld:pubmed |
pubmed-article:15355975 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:15355975 | pubmed:day | 29 | lld:pubmed |
pubmed-article:15355975 | pubmed:volume | 279 | lld:pubmed |
pubmed-article:15355975 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:15355975 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:15355975 | pubmed:pagination | 45300-3 | lld:pubmed |
pubmed-article:15355975 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
pubmed-article:15355975 | pubmed:meshHeading | pubmed-meshheading:15355975... | lld:pubmed |
pubmed-article:15355975 | pubmed:meshHeading | pubmed-meshheading:15355975... | lld:pubmed |
pubmed-article:15355975 | pubmed:meshHeading | pubmed-meshheading:15355975... | lld:pubmed |
pubmed-article:15355975 | pubmed:meshHeading | pubmed-meshheading:15355975... | lld:pubmed |
pubmed-article:15355975 | pubmed:meshHeading | pubmed-meshheading:15355975... | lld:pubmed |
pubmed-article:15355975 | pubmed:meshHeading | pubmed-meshheading:15355975... | lld:pubmed |
pubmed-article:15355975 | pubmed:year | 2004 | lld:pubmed |
pubmed-article:15355975 | pubmed:articleTitle | Regulation of PTEN phosphorylation and stability by a tumor suppressor candidate protein. | lld:pubmed |
pubmed-article:15355975 | pubmed:affiliation | Department of Pharmacology, Tokyo Metropolitan Institute of Medical Science, 3-18-22 Honkomagome, Bunkyo-ku, Tokyo 113-8613, Japan. | lld:pubmed |
pubmed-article:15355975 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:15355975 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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