Intramolecular Regulatory Switch in ZAP-70: Analogy with Receptor Tyrosine Kinases
نویسندگان
چکیده
منابع مشابه
Analogous regulatory sites within the αC-β4 loop regions of ZAP-70 tyrosine kinase and AGC kinases
The precise positioning of the flexible C-helix in the catalytic core is a critical step in the activation of most protein kinases. Consequently, the αC-β4 loop, which anchors the C-helix to the catalytic core, is highly conserved and mediates key structural interactions that serve as a hinge for C-helix movement. While these hinge interactions are conserved across diverse eukaryotic protein ki...
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Engagement of the T cell antigen receptor (TCR) results in activation of several tyrosine kinases leading to tyrosine phosphorylation of protein substrates and activation of multiple biochemical pathways. TCR-mediated activation of the src-family kinases, Lck and Fyn, results in tyrosine phosphorylation of the TCR zeta and CD3 chains. The site of phosphorylation in these chains is the tyrosine-...
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Engagement of the high-affinity IgG Fc receptor (FcgRI) actiSyk nor MAP kinase activation was affected by the presence of ZAP-70. Although transduced ZAP-70 had in vitro kinase vates a signal transduction pathway involving tyrosine phosphorylation of associated kinases. We compared the activity and associated with FceRIg after receptor aggregation, it was not tyrosine phosphorylated. In contras...
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Syk and Zap-70 are related protein-tyrosine kinases implicated in antigen and Fc receptor signaling. While Zap-70 is restricted to T-cells and natural killer cells, Syk accumulates in B-cells, mast cells, platelets, and immature T-cells. In addition, we found that an isoform of Syk (SykB), which carries a 23-amino acid deletion in the "linker" region, is prominently expressed in bone marrow. To...
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Despite extensive study, several of the major components involved in T cell receptor-mediated signaling remain unidentified. Here we report the cloning of the cDNA for a highly tyrosine-phosphorylated 36-38 kDa protein, previously characterized by its association with Grb2, phospholipase C-gamma1, and the p85 subunit of phosphoinositide 3-kinase. Deduced amino acid sequence identifies a novel i...
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ژورنال
عنوان ژورنال: Molecular and Cellular Biology
سال: 2005
ISSN: 0270-7306,1098-5549
DOI: 10.1128/mcb.25.12.4924-4933.2005