| pubmed-article:11533658 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11533658 | lifeskim:mentions | umls-concept:C0105770 | lld:lifeskim |
| pubmed-article:11533658 | lifeskim:mentions | umls-concept:C0162832 | lld:lifeskim |
| pubmed-article:11533658 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:11533658 | lifeskim:mentions | umls-concept:C1418582 | lld:lifeskim |
| pubmed-article:11533658 | lifeskim:mentions | umls-concept:C0243127 | lld:lifeskim |
| pubmed-article:11533658 | lifeskim:mentions | umls-concept:C0475264 | lld:lifeskim |
| pubmed-article:11533658 | lifeskim:mentions | umls-concept:C0021469 | lld:lifeskim |
| pubmed-article:11533658 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:11533658 | lifeskim:mentions | umls-concept:C0443331 | lld:lifeskim |
| pubmed-article:11533658 | pubmed:issue | 9 | lld:pubmed |
| pubmed-article:11533658 | pubmed:dateCreated | 2001-9-4 | lld:pubmed |
| pubmed-article:11533658 | pubmed:abstractText | Phosphorylation on a serine or threonine residue preceding proline (Ser/Thr-Pro) is a key regulatory mechanism, and the conformation of certain phosphorylated Ser/Thr-Pro bonds is regulated specifically by the prolyl isomerase Pin1. Whereas the inhibition of Pin1 induces apoptosis, Pin1 is strikingly overexpressed in a subset of human tumours. Here we show that Pin1 regulates beta-catenin turnover and subcellular localization by interfering with its interaction with adenomatous polyposis coli protein (APC). A differential-display screen reveals that Pin1 increases the transcription of several beta-catenin target genes, including those encoding cyclin D1 and c-Myc. Manipulation of Pin1 levels affects the stability of beta-catenin in vitro. Furthermore, beta-catenin levels are decreased in Pin1-deficient mice but are increased and correlated with Pin1 overexpression in human breast cancer. Pin1 directly binds a phosphorylated Ser-Pro motif next to the APC-binding site in beta-catenin, inhibits its interaction with APC and increases its translocation into the nucleus. Thus, Pin1 is a novel regulator of beta-catenin signalling and its overexpression might contribute to the upregulation of beta-catenin in tumours such as breast cancer, in which APC or beta-catenin mutations are not common. | lld:pubmed |
| pubmed-article:11533658 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11533658 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11533658 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11533658 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11533658 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11533658 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:11533658 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11533658 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11533658 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:11533658 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11533658 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11533658 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:11533658 | pubmed:issn | 1465-7392 | lld:pubmed |
| pubmed-article:11533658 | pubmed:author | pubmed-author:NakamuraMM | lld:pubmed |
| pubmed-article:11533658 | pubmed:author | pubmed-author:WulfGG | lld:pubmed |
| pubmed-article:11533658 | pubmed:author | pubmed-author:LoK FKF | lld:pubmed |
| pubmed-article:11533658 | pubmed:author | pubmed-author:RysEE | lld:pubmed |
| pubmed-article:11533658 | pubmed:author | pubmed-author:LiouY CYC | lld:pubmed |
| pubmed-article:11533658 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11533658 | pubmed:volume | 3 | lld:pubmed |
| pubmed-article:11533658 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11533658 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11533658 | pubmed:pagination | 793-801 | lld:pubmed |
| pubmed-article:11533658 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:11533658 | pubmed:meshHeading | pubmed-meshheading:11533658... | lld:pubmed |
| pubmed-article:11533658 | pubmed:year | 2001 | lld:pubmed |
| pubmed-article:11533658 | pubmed:articleTitle | Pin1 regulates turnover and subcellular localization of beta-catenin by inhibiting its interaction with APC. | lld:pubmed |
| pubmed-article:11533658 | pubmed:affiliation | Cancer Biology Program, Division of Hematology/Oncology, Department of Medicine, Beth Israel Deaconess Medical Center, 330 Brookline Avenue, HIM 1047, Boston, MA 02215, USA. | lld:pubmed |
| pubmed-article:11533658 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11533658 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:11533658 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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