TY - JOUR
T1 - Lck regulates the tyrosine phosphorylation of the T cell receptor subunits and ZAP-70 in murine thymocytes
AU - Van Oers, Nicolai S C
AU - Killeen, Nigel
AU - Weiss, Arthur
PY - 1996/3/1
Y1 - 1996/3/1
N2 - The Src-family and Syk/ZAP-70 family of protein tyrosine kinases (PTK) are required for T cell receptor (TCR) functions. We provide evidence that the Src-family PTK Lck is responsible for regulating the constitutive tyrosine phosphorylation of the TCR ζ subunit in murine thymocytes. Moreover, ligation of the TCR expressed on thymocytes from Lck-deficient mice largely failed to induce the phosphorylation of TCR-ζ, CD3ε, or ZAP-70. In contrast, we find that the TCR-ζ subunit is weakly constitutively tyrosine phosphorylated in peripheral T cells isolated from Lck-null mice. These data suggest that Lck has a functional role in regulation of TCR signal transduction in thymocytes. In peripheral T cells, other Src-family PTKs such as Fyn may partially compensate for the absence of Lck.
AB - The Src-family and Syk/ZAP-70 family of protein tyrosine kinases (PTK) are required for T cell receptor (TCR) functions. We provide evidence that the Src-family PTK Lck is responsible for regulating the constitutive tyrosine phosphorylation of the TCR ζ subunit in murine thymocytes. Moreover, ligation of the TCR expressed on thymocytes from Lck-deficient mice largely failed to induce the phosphorylation of TCR-ζ, CD3ε, or ZAP-70. In contrast, we find that the TCR-ζ subunit is weakly constitutively tyrosine phosphorylated in peripheral T cells isolated from Lck-null mice. These data suggest that Lck has a functional role in regulation of TCR signal transduction in thymocytes. In peripheral T cells, other Src-family PTKs such as Fyn may partially compensate for the absence of Lck.
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U2 - 10.1084/jem.183.3.1053
DO - 10.1084/jem.183.3.1053
M3 - Article
C2 - 8642247
AN - SCOPUS:0029866039
SN - 0022-1007
VL - 183
SP - 1053
EP - 1062
JO - Journal of Experimental Medicine
JF - Journal of Experimental Medicine
IS - 3
ER -