| pubmed-article:16798748 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16798748 | lifeskim:mentions | umls-concept:C0105770 | lld:lifeskim |
| pubmed-article:16798748 | lifeskim:mentions | umls-concept:C0032580 | lld:lifeskim |
| pubmed-article:16798748 | lifeskim:mentions | umls-concept:C0007102 | lld:lifeskim |
| pubmed-article:16798748 | lifeskim:mentions | umls-concept:C0031715 | lld:lifeskim |
| pubmed-article:16798748 | lifeskim:mentions | umls-concept:C0334227 | lld:lifeskim |
| pubmed-article:16798748 | lifeskim:mentions | umls-concept:C1519751 | lld:lifeskim |
| pubmed-article:16798748 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:16798748 | pubmed:issue | 26 | lld:pubmed |
| pubmed-article:16798748 | pubmed:dateCreated | 2006-6-26 | lld:pubmed |
| pubmed-article:16798748 | pubmed:abstractText | Most colorectal cancers have mutations of the adenomatous polyposis coli (APC) gene or the beta-catenin gene that stabilize beta-catenin and activate beta-catenin target genes, leading ultimately to cancer. The molecular mechanisms of APC function in beta-catenin degradation are not completely known. APC binds beta-catenin and is involved in the Axin complex, suggesting that APC regulates beta-catenin phosphorylation. Some evidence also suggests that APC regulates beta-catenin nuclear export. Here, we examine the effects of APC mutations on beta-catenin phosphorylation, ubiquitination, and degradation in the colon cancer cell lines SW480, DLD-1, and HT29, each of which contains a different APC truncation. Although the current models suggest that beta-catenin phosphorylation should be inhibited by APC mutations, we detected significant beta-catenin phosphorylation in these cells. However, beta-catenin ubiquitination and degradation were inhibited in SW480 but not in DLD-1 and HT29 cells. The ubiquitination ofbeta-catenin in SW480 cells can be rescued by exogenous expression of APC. The APC domains required for beta-catenin ubiquitination were analyzed. Our results suggest that APC regulates beta-catenin phosphorylation and ubiquitination by distinct domains and by separate molecular mechanisms. | lld:pubmed |
| pubmed-article:16798748 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16798748 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16798748 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16798748 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:16798748 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16798748 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16798748 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16798748 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16798748 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:16798748 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:16798748 | pubmed:author | pubmed-author:AliD NDN | lld:pubmed |
| pubmed-article:16798748 | pubmed:author | pubmed-author:ZhangWenW | lld:pubmed |
| pubmed-article:16798748 | pubmed:author | pubmed-author:YangJunJ | lld:pubmed |
| pubmed-article:16798748 | pubmed:author | pubmed-author:ChenXiX | lld:pubmed |
| pubmed-article:16798748 | pubmed:author | pubmed-author:LiuChunmingC | lld:pubmed |
| pubmed-article:16798748 | pubmed:author | pubmed-author:EvansPaul MPM | lld:pubmed |
| pubmed-article:16798748 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16798748 | pubmed:day | 30 | lld:pubmed |
| pubmed-article:16798748 | pubmed:volume | 281 | lld:pubmed |
| pubmed-article:16798748 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16798748 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16798748 | pubmed:pagination | 17751-7 | lld:pubmed |
| pubmed-article:16798748 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:16798748 | pubmed:meshHeading | pubmed-meshheading:16798748... | lld:pubmed |
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| pubmed-article:16798748 | pubmed:meshHeading | pubmed-meshheading:16798748... | lld:pubmed |
| pubmed-article:16798748 | pubmed:meshHeading | pubmed-meshheading:16798748... | lld:pubmed |
| pubmed-article:16798748 | pubmed:meshHeading | pubmed-meshheading:16798748... | lld:pubmed |
| pubmed-article:16798748 | pubmed:meshHeading | pubmed-meshheading:16798748... | lld:pubmed |
| pubmed-article:16798748 | pubmed:meshHeading | pubmed-meshheading:16798748... | lld:pubmed |
| pubmed-article:16798748 | pubmed:meshHeading | pubmed-meshheading:16798748... | lld:pubmed |
| pubmed-article:16798748 | pubmed:meshHeading | pubmed-meshheading:16798748... | lld:pubmed |
| pubmed-article:16798748 | pubmed:meshHeading | pubmed-meshheading:16798748... | lld:pubmed |
| pubmed-article:16798748 | pubmed:meshHeading | pubmed-meshheading:16798748... | lld:pubmed |
| pubmed-article:16798748 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:16798748 | pubmed:articleTitle | Adenomatous polyposis coli (APC) differentially regulates beta-catenin phosphorylation and ubiquitination in colon cancer cells. | lld:pubmed |
| pubmed-article:16798748 | pubmed:affiliation | Sealy Center for Cancer Cell Biology and Department of Biochemistry and Molecular Biology, University of Texas Medical Branch, Galveston, TX 77555, USA. | lld:pubmed |
| pubmed-article:16798748 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16798748 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:16798748 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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