| pubmed-article:9482734 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9482734 | lifeskim:mentions | umls-concept:C0105770 | lld:lifeskim |
| pubmed-article:9482734 | lifeskim:mentions | umls-concept:C0031715 | lld:lifeskim |
| pubmed-article:9482734 | lifeskim:mentions | umls-concept:C0033414 | lld:lifeskim |
| pubmed-article:9482734 | lifeskim:mentions | umls-concept:C0205160 | lld:lifeskim |
| pubmed-article:9482734 | lifeskim:mentions | umls-concept:C1332359 | lld:lifeskim |
| pubmed-article:9482734 | lifeskim:mentions | umls-concept:C0244988 | lld:lifeskim |
| pubmed-article:9482734 | lifeskim:mentions | umls-concept:C1520113 | lld:lifeskim |
| pubmed-article:9482734 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
| pubmed-article:9482734 | lifeskim:mentions | umls-concept:C0376315 | lld:lifeskim |
| pubmed-article:9482734 | lifeskim:mentions | umls-concept:C1704735 | lld:lifeskim |
| pubmed-article:9482734 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:9482734 | pubmed:dateCreated | 1998-4-16 | lld:pubmed |
| pubmed-article:9482734 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9482734 | pubmed:abstractText | Glycogen synthase kinase-3 (GSK-3) mediates epidermal growth factor, insulin and Wnt signals to various downstream events such as glycogen metabolism, gene expression, proliferation and differentiation. We have isolated here a GSK-3beta-interacting protein from a rat brain cDNA library using a yeast two-hybrid method. This protein consists of 832 amino acids and possesses Regulators of G protein Signaling (RGS) and dishevelled (Dsh) homologous domains in its N- and C-terminal regions, respectively. The predicted amino acid sequence of this GSK-3beta-interacting protein shows 94% identity with mouse Axin, which recently has been identified as a negative regulator of the Wnt signaling pathway; therefore, we termed this protein rAxin (rat Axin). rAxin interacted directly with, and was phosphorylated by, GSK-3beta. rAxin also interacted directly with the armadillo repeats of beta-catenin. The binding site of rAxin for GSK-3beta was distinct from the beta-catenin-binding site, and these three proteins formed a ternary complex. Furthermore, rAxin promoted GSK-3beta-dependent phosphorylation of beta-catenin. These results suggest that rAxin negatively regulates the Wnt signaling pathway by interacting with GSK-3beta and beta-catenin and mediating the signal from GSK-3beta to beta-catenin. | lld:pubmed |
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| pubmed-article:9482734 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9482734 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9482734 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:9482734 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9482734 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9482734 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9482734 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9482734 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9482734 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:9482734 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9482734 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:9482734 | pubmed:issn | 0261-4189 | lld:pubmed |
| pubmed-article:9482734 | pubmed:author | pubmed-author:YamamotoHH | lld:pubmed |
| pubmed-article:9482734 | pubmed:author | pubmed-author:IkedaSS | lld:pubmed |
| pubmed-article:9482734 | pubmed:author | pubmed-author:KoyamaSS | lld:pubmed |
| pubmed-article:9482734 | pubmed:author | pubmed-author:KikuchiAA | lld:pubmed |
| pubmed-article:9482734 | pubmed:author | pubmed-author:KishidaSS | lld:pubmed |
| pubmed-article:9482734 | pubmed:author | pubmed-author:MuraiHH | lld:pubmed |
| pubmed-article:9482734 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9482734 | pubmed:day | 2 | lld:pubmed |
| pubmed-article:9482734 | pubmed:volume | 17 | lld:pubmed |
| pubmed-article:9482734 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9482734 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9482734 | pubmed:pagination | 1371-84 | lld:pubmed |
| pubmed-article:9482734 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
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