Jurkat细胞
锡克
NFAT公司
ZAP70型
T细胞
T细胞受体
细胞生物学
酪氨酸磷酸化
生物
磷酸化
分子生物学
MAPK/ERK通路
信号转导
酪氨酸激酶
转录因子
生物化学
免疫学
免疫系统
基因
作者
Maria Paola Martelli,Huamao Mark Lin,Weiguo Zhang,Lawrence E. Samelson,Barbara E. Bierer
出处
期刊:Blood
[American Society of Hematology]
日期:2000-09-15
卷期号:96 (6): 2181-2190
被引量:51
标识
DOI:10.1182/blood.v96.6.2181
摘要
Abstract Activation of T cells can be initiated through cell surface molecules in addition to the T-cell receptor-CD3 (TCR-CD3) complex. In human T cells, ligation of the CD2 molecule by mitogenic pairs of anti-CD2 monoclonal antibodies activates T cells via biochemical signaling pathways similar but not identical to those elicited on TCR engagement. This study describes a key role for the p36/38 membrane adapter protein linker for T cell activation (LAT) in CD2-mediated T-cell activation. Following ligation of CD2 on the surface of the Jurkat T-cell line and human purified T cells, LAT was tyrosine phosphorylated and shown to associate in vivo with a number of other tyrosine phosphorylated proteins including PLCγ-1, Grb-2, and SLP-76. Using Jurkat cell lines deficient in ZAP70/Syk (P116) or LAT (ANJ3) expression, CD2-dependent PLCγ-1 and SLP-76 tyrosine phosphorylation required expression both of ZAP70 or Syk and of LAT. As predicted, the absence of either LAT or ZAP70/Syk kinases correlated with a defect in the induction of nuclear factor of activated T cells (NFAT) transcriptional activity, activation of the interleukin-2 promoter, and ERK phosphorylation following CD2 stimulation. These data suggest that LAT is an adapter protein important for the regulation of CD2-mediated T-cell activation.
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