| pubmed-article:7685905 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7685905 | lifeskim:mentions | umls-concept:C0021756 | lld:lifeskim |
| pubmed-article:7685905 | lifeskim:mentions | umls-concept:C0041485 | lld:lifeskim |
| pubmed-article:7685905 | lifeskim:mentions | umls-concept:C0139030 | lld:lifeskim |
| pubmed-article:7685905 | lifeskim:mentions | umls-concept:C1150423 | lld:lifeskim |
| pubmed-article:7685905 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:7685905 | lifeskim:mentions | umls-concept:C0205132 | lld:lifeskim |
| pubmed-article:7685905 | lifeskim:mentions | umls-concept:C0441712 | lld:lifeskim |
| pubmed-article:7685905 | pubmed:issue | 12 | lld:pubmed |
| pubmed-article:7685905 | pubmed:dateCreated | 1993-7-22 | lld:pubmed |
| pubmed-article:7685905 | pubmed:abstractText | Previously we found that interleukin 2 (IL-2) induces tyrosine phosphorylation and activation of the serine/threonine-specific kinase encoded by the raf-1 protooncogene in a T-cell line, CTLL-2. Here we extended these findings by exploring the effects of selective removal of phosphate from tyrosines in p72-74-Raf-1 kinase that had been immunoprecipitated from IL-2-stimulated CTLL-2 cells. Treatment in vitro of IL-2-activated Raf-1 with the tyrosine-specific phosphatases CD45 and TCPTP (formerly called T-cell protein tyrosine phosphatase) reduced Raf kinase activity to nearly baseline levels. This effect was completely inhibited by the phosphatase inhibitor sodium orthovanadate. In contrast, treatment of Raf-1 with a serine/threonine-specific phosphatase, protein phosphatase 1 (PP-1), resulted in a more modest decrease in Raf in vitro kinase activity, and this effect was prevented by okadaic acid. Two-dimensional phosphoamino acid analysis confirmed the selective removal of phosphate from tyrosine by CD45 and from serine and threonine by PP-1. The immunoreactivity of p72-74-Raf-1 with anti-phosphotyrosine antibodies was also completely abolished by treatment with CD45 in the absence but not in the presence of sodium orthovanadate. These findings provide evidence that the IL-2-stimulated phosphorylation of Raf-1 on tyrosines plays an important role in upregulating the activity of this serine/threonine-specific kinase in CTLL-2 cells and, as such, provides a model system for studying the transfer of growth factor-initiated signals from protein tyrosine kinases to serine/threonine-specific kinases. | lld:pubmed |
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| pubmed-article:7685905 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:7685905 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:7685905 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7685905 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:7685905 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:7685905 | pubmed:author | pubmed-author:ReedJ CJC | lld:pubmed |
| pubmed-article:7685905 | pubmed:author | pubmed-author:RappU RUR | lld:pubmed |
| pubmed-article:7685905 | pubmed:author | pubmed-author:TurnerB CBC | lld:pubmed |
| pubmed-article:7685905 | pubmed:author | pubmed-author:TonksN KNK | lld:pubmed |
| pubmed-article:7685905 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7685905 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:7685905 | pubmed:volume | 90 | lld:pubmed |
| pubmed-article:7685905 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7685905 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7685905 | pubmed:pagination | 5544-8 | lld:pubmed |
| pubmed-article:7685905 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:7685905 | pubmed:year | 1993 | lld:pubmed |
| pubmed-article:7685905 | pubmed:articleTitle | Interleukin 2 regulates Raf-1 kinase activity through a tyrosine phosphorylation-dependent mechanism in a T-cell line. | lld:pubmed |
| pubmed-article:7685905 | pubmed:affiliation | Department of Pathology and Laboratory Medicine, University of Pennsylvania School of Medicine, Philadelphia 19104-6082. | lld:pubmed |
| pubmed-article:7685905 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7685905 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:7685905 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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