| pubmed-article:11927552 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11927552 | lifeskim:mentions | umls-concept:C0597357 | lld:lifeskim |
| pubmed-article:11927552 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:11927552 | lifeskim:mentions | umls-concept:C0037083 | lld:lifeskim |
| pubmed-article:11927552 | lifeskim:mentions | umls-concept:C0050668 | lld:lifeskim |
| pubmed-article:11927552 | lifeskim:mentions | umls-concept:C1414387 | lld:lifeskim |
| pubmed-article:11927552 | lifeskim:mentions | umls-concept:C1710082 | lld:lifeskim |
| pubmed-article:11927552 | lifeskim:mentions | umls-concept:C0086597 | lld:lifeskim |
| pubmed-article:11927552 | pubmed:issue | 7 | lld:pubmed |
| pubmed-article:11927552 | pubmed:dateCreated | 2002-4-2 | lld:pubmed |
| pubmed-article:11927552 | pubmed:abstractText | Activins, members of the transforming growth factor-beta family, are pleiotropic growth and differentiation factors. Activin A induces B-cell apoptosis. To identify the genes responsible for activin-induced apoptosis, we performed retrovirus-mediated gene trap screening in a mouse B-cell line. We identified the rasGAP-binding protein Dok-1 (p62) as an essential molecule that links activin receptors with Smad proteins. In B cells overexpressing Dok-1, activin A-induced apoptotic responses were augmented. The expression of bcl-X(L) was down-regulated by inhibition of the ras/Erk pathway. Activin stimulation triggered association of Dok-1 with Smad3, as well as association of Smad3 with Smad4. Dok-1 also associated with both the type I and type II activin receptors. Dok-1 has been characterized previously as a tyrosine-phosphorylated protein acting downstream of the protein tyrosine kinase pathway: intriguingly, activin signaling did not induce tyrosine phosphorylation of Dok-1. These findings indicate that Dok-1 acts as an adaptor protein that links the activin receptors with the Smads, suggesting a novel function for Dok-1 in activin signaling leading to B-cell apoptosis. | lld:pubmed |
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| pubmed-article:11927552 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11927552 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11927552 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11927552 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:11927552 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11927552 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:11927552 | pubmed:issn | 0261-4189 | lld:pubmed |
| pubmed-article:11927552 | pubmed:author | pubmed-author:TsuchidaKunih... | lld:pubmed |
| pubmed-article:11927552 | pubmed:author | pubmed-author:SuginoHiromuH | lld:pubmed |
| pubmed-article:11927552 | pubmed:author | pubmed-author:YamakawaNorio... | lld:pubmed |
| pubmed-article:11927552 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11927552 | pubmed:day | 2 | lld:pubmed |
| pubmed-article:11927552 | pubmed:volume | 21 | lld:pubmed |
| pubmed-article:11927552 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11927552 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11927552 | pubmed:pagination | 1684-94 | lld:pubmed |
| pubmed-article:11927552 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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