| pubmed-article:8947046 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8947046 | lifeskim:mentions | umls-concept:C0031715 | lld:lifeskim |
| pubmed-article:8947046 | lifeskim:mentions | umls-concept:C0178539 | lld:lifeskim |
| pubmed-article:8947046 | lifeskim:mentions | umls-concept:C0292688 | lld:lifeskim |
| pubmed-article:8947046 | lifeskim:mentions | umls-concept:C1704632 | lld:lifeskim |
| pubmed-article:8947046 | lifeskim:mentions | umls-concept:C0871261 | lld:lifeskim |
| pubmed-article:8947046 | lifeskim:mentions | umls-concept:C2911692 | lld:lifeskim |
| pubmed-article:8947046 | lifeskim:mentions | umls-concept:C1706817 | lld:lifeskim |
| pubmed-article:8947046 | pubmed:issue | 22 | lld:pubmed |
| pubmed-article:8947046 | pubmed:dateCreated | 1997-1-9 | lld:pubmed |
| pubmed-article:8947046 | pubmed:abstractText | Transforming growth factor-beta (TGF-beta) signals via an oligomeric complex of two serine/threonine kinase receptors denoted TGF-beta type I receptor (TbetaR-I) and type II receptor (TbetaR-II). We investigated the in vivo phosphorylation sites in TbetaR-I and TbetaR-II after complex formation. Phosphorylation of TbetaR-II was observed at residues in the C-terminus (Ser549 and Ser551) and at residues in the juxtamembrane domain (Ser223, Ser226 and Ser227). TGF-beta1 induced in vivo phosphorylation of serine and threonine residues in the juxtamembrane domain of TbetaR-I in a region rich in glycine, serine and threonine residues (GS domain; Thr185, Thr186, Ser187, Ser189 and Ser191), and more N-terminal of this region (Ser165). Phosphorylation in the GS domain has been shown previously to be involved in activation of the TbetaR-I kinase. We show here that phosphorylation of TbetaR-I at Ser165 is involved in modulation of TGF-beta1 signaling. Mutations of Ser165 in TbetaR-I led to an increase in TGF-beta1-mediated growth inhibition and extracellular matrix formation, but, in contrast, to decreased TGF-beta1-induced apoptosis. A transcriptional activation signal was not affected. Mutations of Ser165 changed the phosphorylation pattern of TbetaR-I. These observations suggest that TGF-beta receptor signaling specificity is modulated by phosphorylation of Ser165 of TbetaR-I. | lld:pubmed |
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| pubmed-article:8947046 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8947046 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8947046 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:8947046 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8947046 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:8947046 | pubmed:issn | 0261-4189 | lld:pubmed |
| pubmed-article:8947046 | pubmed:author | pubmed-author:HeldinC HCH | lld:pubmed |
| pubmed-article:8947046 | pubmed:author | pubmed-author:MiyazonoKK | lld:pubmed |
| pubmed-article:8947046 | pubmed:author | pubmed-author:ten DijkePP | lld:pubmed |
| pubmed-article:8947046 | pubmed:author | pubmed-author:Souchelnytsky... | lld:pubmed |
| pubmed-article:8947046 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8947046 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:8947046 | pubmed:volume | 15 | lld:pubmed |
| pubmed-article:8947046 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8947046 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8947046 | pubmed:pagination | 6231-40 | lld:pubmed |
| pubmed-article:8947046 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:8947046 | pubmed:year | 1996 | lld:pubmed |
| pubmed-article:8947046 | pubmed:articleTitle | Phosphorylation of Ser165 in TGF-beta type I receptor modulates TGF-beta1-induced cellular responses. | lld:pubmed |
| pubmed-article:8947046 | pubmed:affiliation | Ludwig Institute for Cancer Research, Uppsala, Sweden. | lld:pubmed |
| pubmed-article:8947046 | pubmed:publicationType | Journal Article | lld:pubmed |
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