TY - JOUR
T1 - Tandem SH2 domains of ZAP-70 bind to T cell antigen receptor ζ and CD3∈ from activated Jurkat T cells
AU - Wange, Ronald L.
AU - Malek, Sami N.
AU - Desiderio, Stephen
AU - Samelson, Lawrence E.
N1 - Copyright:
Copyright 2004 Elsevier B.V., All rights reserved.
PY - 1993/9/15
Y1 - 1993/9/15
N2 - A proximal and critical biochemical event upon T cell antigen receptor (TCR) stimulation is the activation of a protein tyrosine kinase (PTK) pathway. ZAP-70, a PTK of the p72syk family, associates with phosphorylated TCR subunits upon TCR stimulation. Here we report that the tandem SH2 domains of ZAP-70, expressed as a fusion protein, bind to tyrosine-phosphorylated CDS3∈ and TCRζ from activated Jurkat T cell lysates. The single N-and C-terminal SH2 domains Of ZAP-70, expressed separately, do not bind these TCR subunits. In comparison to fusion proteins containing SH2 domains from other proteins, the tandem SH2 domains of ZAP-70 demonstrate a remarkably restricted repertoire of protein binding, binding only TCRζ and CD3∈. ZAP-70 is also recovered in the binding assay, but this is likely to be a consequence of its interaction with multiple SH2 binding sites on the ζ-ζ and CD3∈-containing dimers.
AB - A proximal and critical biochemical event upon T cell antigen receptor (TCR) stimulation is the activation of a protein tyrosine kinase (PTK) pathway. ZAP-70, a PTK of the p72syk family, associates with phosphorylated TCR subunits upon TCR stimulation. Here we report that the tandem SH2 domains of ZAP-70, expressed as a fusion protein, bind to tyrosine-phosphorylated CDS3∈ and TCRζ from activated Jurkat T cell lysates. The single N-and C-terminal SH2 domains Of ZAP-70, expressed separately, do not bind these TCR subunits. In comparison to fusion proteins containing SH2 domains from other proteins, the tandem SH2 domains of ZAP-70 demonstrate a remarkably restricted repertoire of protein binding, binding only TCRζ and CD3∈. ZAP-70 is also recovered in the binding assay, but this is likely to be a consequence of its interaction with multiple SH2 binding sites on the ζ-ζ and CD3∈-containing dimers.
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M3 - Article
C2 - 8366117
AN - SCOPUS:0027328526
SN - 0021-9258
VL - 268
SP - 19797
EP - 19801
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 26
ER -