| pubmed-article:8901551 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8901551 | lifeskim:mentions | umls-concept:C1705831 | lld:lifeskim |
| pubmed-article:8901551 | lifeskim:mentions | umls-concept:C1527940 | lld:lifeskim |
| pubmed-article:8901551 | lifeskim:mentions | umls-concept:C1421567 | lld:lifeskim |
| pubmed-article:8901551 | lifeskim:mentions | umls-concept:C1264638 | lld:lifeskim |
| pubmed-article:8901551 | lifeskim:mentions | umls-concept:C0243102 | lld:lifeskim |
| pubmed-article:8901551 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:8901551 | lifeskim:mentions | umls-concept:C0441712 | lld:lifeskim |
| pubmed-article:8901551 | pubmed:issue | 22 | lld:pubmed |
| pubmed-article:8901551 | pubmed:dateCreated | 1996-12-24 | lld:pubmed |
| pubmed-article:8901551 | pubmed:abstractText | There is a growing body of evidence, including data from human genetic and T-cell receptor function studies, which implicate a zeta-associated protein of M(r) 70,000 (Zap-70) as a critical protein tyrosine kinase in T-cell activation and development. During T-cell activation, Zap-70 becomes associated via its src homology type 2 (SH2) domains with tyrosine-phosphorylated immune-receptor tyrosine activating motif (ITAM) sequences in the cytoplasmic zeta chain of the T-cell receptor. An intriguing conundrum is how Zap-70 is catalytically activated for downstream phosphorylation events. To address this question, we have used purified Zap-70, tyrosine phosphorylated glutathione S-transferase (GST)-Zeta, and GST-Zeta-1 cytoplasmic domains, and various forms of ITAM-containing peptides to see what effect binding of zeta had upon Zap-70 tyrosine kinase activity. The catalytic activity of Zap-70 with respect to autophosphorylation increased approximately 5-fold in the presence of 125 nM phosphorylated GST-Zeta or GST-Zeta-1 cytoplasmic domain. A 20-fold activity increase was observed for phosphorylation of an exogenous substrate. Both activity increases showed a GST-Zeta concentration dependence. The increase in activity was not produced with nonphosphorylated GST-Zeta, phosphorylated zeta, or phosphorylated ITAM-containing peptides. The increase in Zap-70 activity was SH2 mediated and was inhibited by phenylphosphate, Zap-70 SH2, and an antibody specific for Zap-70 SH2 domains. Since GST-Zeta and GST-Zeta-1 exist as dimers, the data suggest Zap-70 is activated upon binding a dimeric form of phosphorylated zeta and not by peptide fragments containing a single phosphorylated ITAM. Taken together, these data indicate that the catalytic activity of Zap-70 is most likely activated by a trans-phosphorylation mechanism. | lld:pubmed |
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| pubmed-article:8901551 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8901551 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8901551 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8901551 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:8901551 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8901551 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:8901551 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:8901551 | pubmed:author | pubmed-author:WisniewskiDD | lld:pubmed |
| pubmed-article:8901551 | pubmed:author | pubmed-author:HawkinsJJ | lld:pubmed |
| pubmed-article:8901551 | pubmed:author | pubmed-author:MarcuEE | lld:pubmed |
| pubmed-article:8901551 | pubmed:author | pubmed-author:LoGrassoP VPV | lld:pubmed |
| pubmed-article:8901551 | pubmed:author | pubmed-author:FrankL JLJ | lld:pubmed |
| pubmed-article:8901551 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8901551 | pubmed:day | 29 | lld:pubmed |
| pubmed-article:8901551 | pubmed:volume | 93 | lld:pubmed |
| pubmed-article:8901551 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8901551 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8901551 | pubmed:pagination | 12165-70 | lld:pubmed |
| pubmed-article:8901551 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:8901551 | pubmed:meshHeading | pubmed-meshheading:8901551-... | lld:pubmed |
| pubmed-article:8901551 | pubmed:year | 1996 | lld:pubmed |
| pubmed-article:8901551 | pubmed:articleTitle | Mechanism of activation for Zap-70 catalytic activity. | lld:pubmed |
| pubmed-article:8901551 | pubmed:affiliation | Department of Molecular Design and Diversity, Merck Research Laboratories, Rahway, NJ 07065, USA. lograsso@merck.com | lld:pubmed |
| pubmed-article:8901551 | pubmed:publicationType | Journal Article | lld:pubmed |
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