Samelson L E, Phillips A F, Luong E T, Klausner R D
Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892.
Proc Natl Acad Sci U S A. 1990 Jun;87(11):4358-62. doi: 10.1073/pnas.87.11.4358.
Activation of the T-cell antigen receptor (TCR) results in tyrosine phosphorylation of the TCR zeta chain and other intracellular substrates. Two other T-cell integral membrane proteins, CD4 and CD8, are associated with the protein-tyrosine kinase (PTK), lck. Despite evidence that activation of this enzyme results in TCR-zeta chain phosphorylation, it has not been shown that the TCR activates lck. We have sought evidence that the TCR is associated with a PTK. In this study we use digitonin to solubilize a murine T-cell hybridoma and demonstrate that antibodies binding extracellular but not intracellular domains of the TCR specifically coprecipitate only the fyn PTK and not lck or yes, two other kinases found in these cells. The association of the fyn PTK with the TCR might enable the T cell to independently regulate two PTKs through surface receptors.
T细胞抗原受体（TCR）的激活会导致TCR ζ链和其他细胞内底物的酪氨酸磷酸化。另外两种T细胞整合膜蛋白CD4和CD8与蛋白酪氨酸激酶（PTK）lck相关联。尽管有证据表明该酶的激活会导致TCR ζ链磷酸化，但尚未证明TCR能激活lck。我们一直在寻找TCR与PTK相关联的证据。在本研究中，我们使用洋地黄皂苷溶解小鼠T细胞杂交瘤，并证明结合TCR细胞外而非细胞内结构域的抗体仅特异性共沉淀fyn PTK，而不共沉淀lck或yes，这是在这些细胞中发现的另外两种激酶。fyn PTK与TCR的关联可能使T细胞能够通过表面受体独立调节两种PTK。
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