| pubmed-article:17636029 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17636029 | lifeskim:mentions | umls-concept:C0037083 | lld:lifeskim |
| pubmed-article:17636029 | lifeskim:mentions | umls-concept:C0062773 | lld:lifeskim |
| pubmed-article:17636029 | lifeskim:mentions | umls-concept:C0001038 | lld:lifeskim |
| pubmed-article:17636029 | lifeskim:mentions | umls-concept:C0205160 | lld:lifeskim |
| pubmed-article:17636029 | lifeskim:mentions | umls-concept:C1334889 | lld:lifeskim |
| pubmed-article:17636029 | lifeskim:mentions | umls-concept:C1333931 | lld:lifeskim |
| pubmed-article:17636029 | lifeskim:mentions | umls-concept:C1710082 | lld:lifeskim |
| pubmed-article:17636029 | lifeskim:mentions | umls-concept:C1704970 | lld:lifeskim |
| pubmed-article:17636029 | lifeskim:mentions | umls-concept:C1551336 | lld:lifeskim |
| pubmed-article:17636029 | lifeskim:mentions | umls-concept:C1704735 | lld:lifeskim |
| pubmed-article:17636029 | pubmed:issue | 18 | lld:pubmed |
| pubmed-article:17636029 | pubmed:dateCreated | 2007-8-31 | lld:pubmed |
| pubmed-article:17636029 | pubmed:abstractText | The Notch signaling pathway appears to perform an important function in a wide variety of organisms and cell types. In our present study, we provide evidence that UV irradiation-induced Tip60 proteins reduced Notch1 activity to a marked degree. Accumulated UV irradiation-induced Tip60 suppresses Notch1 transcriptional activity via the dissociation of the Notch1-IC-CSL complex. The binding between endogenous Tip60 and Notch1-IC in UV radiation-exposed cells was verified in this study by coimmunoprecipitation. Interestingly, the physical interaction of Tip60 with Notch1-IC occurs to a more profound degree in the presence of CSL but does not exist in a trimeric complex. Using Notch1-IC and Tip60 deletion mutants, we also determined that the N terminus, which harbors the RAM domain and seven ankyrin repeats of Notch1-IC, interacts with the zinc finger and acetyl coenzyme A domains of Tip60. Furthermore, here we report that Notch1-IC is a direct target of the acetyltransferase activity of Tip60. Collectively, our data suggest that Tip60 is an inhibitor of the Notch1 signaling pathway and that Tip60-dependent acetylation of Notch1-IC may be relevant to the mechanism by which Tip60 suppresses Notch1 signaling. | lld:pubmed |
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| pubmed-article:17636029 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17636029 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17636029 | pubmed:citationSubset | IM | lld:pubmed |
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