Source:http://linkedlifedata.com/resource/pubmed/id/18586027
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
15
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| pubmed:dateCreated |
2008-9-1
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| pubmed:abstractText |
Beta-catenin plays a role in intracellular adhesion and regulating gene expression. The latter role is associated with its oncogenic properties. Phosphorylation of beta-catenin controls its intracellular expression but mechanism/s that regulates the nuclear localization of beta-catenin is unknown. We demonstrate that O-GlcNAc glycosylation (O-GlcNAcylation) of beta-catenin negatively regulates its levels in the nucleus. We show that normal prostate cells (PNT1A) have significantly higher amounts of O-GlcNAcylated beta-catenin compared to prostate cancer (CaP) cells. The total nuclear levels of beta-catenin are higher in the CaP cells than PNT1A but only a minimal fraction of the nuclear beta-catenin in the CaP cells are O-GlcNAcylated. Increasing the levels of O-GlcNAcylated beta-catenin in the CaP cells with PUGNAc (O- (2-acetamido-2-deoxy-d-gluco-pyranosylidene) amino-N-phenylcarbamate) treatment is associated with a progressive decrease in the levels of beta-catenin in the nucleus. TOPFlash reporter assay and mRNA expressions of beta-catenin's target genes indicate that O-GlcNAcylation of beta-catenin results in a decrease in its transcriptional activity. We define a novel modification of beta-catenin that regulates its nuclear localization and transcriptional function.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Acetylglucosamine,
http://linkedlifedata.com/resource/pubmed/chemical/N-Acetylglucosaminyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/O-GlcNAc transferase,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/beta Catenin
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| pubmed:status |
MEDLINE
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| pubmed:month |
Sep
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| pubmed:issn |
1090-2422
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| pubmed:author | |
| pubmed:issnType |
Electronic
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| pubmed:day |
10
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| pubmed:volume |
314
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| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
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| pubmed:pagination |
2774-87
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| pubmed:dateRevised |
2008-11-21
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| pubmed:meshHeading |
pubmed-meshheading:18586027-Acetylglucosamine,
pubmed-meshheading:18586027-Active Transport, Cell Nucleus,
pubmed-meshheading:18586027-Carcinoma,
pubmed-meshheading:18586027-Cell Adhesion,
pubmed-meshheading:18586027-Cell Line,
pubmed-meshheading:18586027-Cell Line, Tumor,
pubmed-meshheading:18586027-Cell Nucleus,
pubmed-meshheading:18586027-Epithelial Cells,
pubmed-meshheading:18586027-Gene Expression Regulation, Neoplastic,
pubmed-meshheading:18586027-Glycosylation,
pubmed-meshheading:18586027-Humans,
pubmed-meshheading:18586027-Male,
pubmed-meshheading:18586027-N-Acetylglucosaminyltransferases,
pubmed-meshheading:18586027-Prostate,
pubmed-meshheading:18586027-Prostatic Neoplasms,
pubmed-meshheading:18586027-RNA, Messenger,
pubmed-meshheading:18586027-Signal Transduction,
pubmed-meshheading:18586027-Transcriptional Activation,
pubmed-meshheading:18586027-Up-Regulation,
pubmed-meshheading:18586027-beta Catenin
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| pubmed:year |
2008
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| pubmed:articleTitle |
O-GlcNAc-glycosylation of beta-catenin regulates its nuclear localization and transcriptional activity.
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| pubmed:affiliation |
Department of Biochemistry and Biomedical Sciences, McMaster University, Hamilton, Ontario, Canada L8N 3Z5.
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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