| pubmed-article:10339577 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10339577 | lifeskim:mentions | umls-concept:C0043342 | lld:lifeskim |
| pubmed-article:10339577 | lifeskim:mentions | umls-concept:C0010222 | lld:lifeskim |
| pubmed-article:10339577 | lifeskim:mentions | umls-concept:C0105770 | lld:lifeskim |
| pubmed-article:10339577 | lifeskim:mentions | umls-concept:C1522496 | lld:lifeskim |
| pubmed-article:10339577 | lifeskim:mentions | umls-concept:C0218349 | lld:lifeskim |
| pubmed-article:10339577 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:10339577 | lifeskim:mentions | umls-concept:C1522492 | lld:lifeskim |
| pubmed-article:10339577 | pubmed:issue | 11 | lld:pubmed |
| pubmed-article:10339577 | pubmed:dateCreated | 1999-6-24 | lld:pubmed |
| pubmed-article:10339577 | pubmed:abstractText | Regulation of beta-catenin stability is essential for Wnt signal transduction during development and tumorigenesis. It is well known that serine-phosphorylation of beta-catenin by the Axin-glycogen synthase kinase (GSK)-3beta complex targets beta-catenin for ubiquitination-degradation, and mutations at critical phosphoserine residues stabilize beta-catenin and cause human cancers. How beta-catenin phosphorylation results in its degradation is undefined. Here we show that phosphorylated beta-catenin is specifically recognized by beta-Trcp, an F-box/WD40-repeat protein that also associates with Skp1, an essential component of the ubiquitination apparatus. beta-catenin harboring mutations at the critical phosphoserine residues escapes recognition by beta-Trcp, thus providing a molecular explanation for why these mutations cause beta-catenin accumulation that leads to cancer. Inhibition of endogenous beta-Trcp function by a dominant negative mutant stabilizes beta-catenin, activates Wnt/beta-catenin signaling, and induces axis formation in Xenopus embryos. Therefore, beta-Trcp plays a central role in recruiting phosphorylated beta-catenin for degradation and in dorsoventral patterning of the Xenopus embryo. | lld:pubmed |
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| pubmed-article:10339577 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10339577 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10339577 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10339577 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10339577 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:10339577 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10339577 | pubmed:month | May | lld:pubmed |
| pubmed-article:10339577 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:10339577 | pubmed:author | pubmed-author:KatoYY | lld:pubmed |
| pubmed-article:10339577 | pubmed:author | pubmed-author:LisMM | lld:pubmed |
| pubmed-article:10339577 | pubmed:author | pubmed-author:HUHH | lld:pubmed |
| pubmed-article:10339577 | pubmed:author | pubmed-author:YanknerB ABA | lld:pubmed |
| pubmed-article:10339577 | pubmed:author | pubmed-author:ZhangZZ | lld:pubmed |
| pubmed-article:10339577 | pubmed:author | pubmed-author:VikPP | lld:pubmed |
| pubmed-article:10339577 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10339577 | pubmed:day | 25 | lld:pubmed |
| pubmed-article:10339577 | pubmed:volume | 96 | lld:pubmed |
| pubmed-article:10339577 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10339577 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10339577 | pubmed:pagination | 6273-8 | lld:pubmed |
| pubmed-article:10339577 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
| pubmed-article:10339577 | pubmed:meshHeading | pubmed-meshheading:10339577... | lld:pubmed |
| pubmed-article:10339577 | pubmed:meshHeading | pubmed-meshheading:10339577... | lld:pubmed |
| pubmed-article:10339577 | pubmed:meshHeading | pubmed-meshheading:10339577... | lld:pubmed |
