TY - JOUR
T1 - ZAP-70 is constitutively associated with tyrosine-phosphorylated TCR ζ in murine thymocytes and lymph node T cells
AU - van Oers, Nicolai S C
AU - Killeen, Nigel
AU - Welss, Arthur
N1 - Funding Information:
This work was supported in part by by grants from the National Institutes of Health (GM39553 to A. W.), and the Human Frontier Science Program Organization (LT-505/93 to N. v. 0.). N. v. 0. is the recipient of a Human Frontier Science Program Post-Doctoral Fellowship Award. N. K. is a special fellow of the Leukemia Society of America. We would like to thank Dr. D. Straus for critical reading of the manuscript and J. Wu and Dr. B. Irving for helpful discussions. We are extremely grateful to Drs. M. Coles and D. Rauiet (University of Caiifor-nia, Berkeley) for kindly providing the MHC-deficient mice necessary for our studies, Dr. D. Littman (University of California. San Francisco) for providing theCD4-deficient mice, and Dr. J. Ravetch (Sioan-Kettering Institute, New York) for the rabbit anti-l; antisera.
PY - 1994/11
Y1 - 1994/11
N2 - Studies with T cell lines and clones have shown that engagement of the TCR results in the tyrosine phosphorylation of the TCR subunits. This leads to the recruitment of the ZAP-70 protein tyrosine kinase, an interaction involving the two SH2-domains of ZAP-70 with tyrosine-phosphorylated ζ and CD3. However, as previously described, murine thymocytes and lymph node T cells express a constitutively tyrosine-phosphorylated ζ subunit in the basal state. Here, we show that a fraction of ZAP-70 molecules are constitutively associated with tyrosine-phosphorylated ζ. TCR ligation promotes a large increase in the tyrosine phosphorylation of ZAP-70 as well as other TCR subunits. Genetic studies reveal that the constitutive ZAP-70 association with tyrosine-phosphorylated ζ does not absolutely require either TCR or coreceptor interactions with MHC molecules.
AB - Studies with T cell lines and clones have shown that engagement of the TCR results in the tyrosine phosphorylation of the TCR subunits. This leads to the recruitment of the ZAP-70 protein tyrosine kinase, an interaction involving the two SH2-domains of ZAP-70 with tyrosine-phosphorylated ζ and CD3. However, as previously described, murine thymocytes and lymph node T cells express a constitutively tyrosine-phosphorylated ζ subunit in the basal state. Here, we show that a fraction of ZAP-70 molecules are constitutively associated with tyrosine-phosphorylated ζ. TCR ligation promotes a large increase in the tyrosine phosphorylation of ZAP-70 as well as other TCR subunits. Genetic studies reveal that the constitutive ZAP-70 association with tyrosine-phosphorylated ζ does not absolutely require either TCR or coreceptor interactions with MHC molecules.
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U2 - 10.1016/1074-7613(94)90038-8
DO - 10.1016/1074-7613(94)90038-8
M3 - Article
C2 - 7600293
AN - SCOPUS:0028535120
SN - 1074-7613
VL - 1
SP - 675
EP - 685
JO - Immunity
JF - Immunity
IS - 8
ER -