Dynamic molecular interactions linking the T cell antigen receptor to the actin cytoskeleton
Dynamic molecular interactions linking the T cell antigen receptor to the actin cytoskeleton
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DOI：
10.1038/ni1143
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发表时间：
2005-01-01
影响因子：
30.5
通讯作者：
Samelson, LE
中科院分区：
文献类型：
--
作者：
Barda-Saad, M;Braiman, A;Samelson, LE
T 细胞受体 (TCR) 接合导致 T 细胞与抗原呈递细胞接触部位发生肌动蛋白聚合。在这里，我们研究了活化后参与调节活 T 细胞肌动蛋白聚合的蛋白质的动态活性。两种这样的衔接蛋白 Nck 和 Wiskott-Aldrich 综合征蛋白 (WASp) 在 T 细胞初始激活过程中被招募到 TCR，并与酪氨酸激酶 Zap70 共定位。 Nck 和 WASp 的募集取决于 TCR 诱导的酪氨酸磷酸化以及 LAT 和 SLP-76 接头。 Nck 和 WASp 向外周迁移并积聚在富含肌动蛋白的圆周环处。因此，受 TCR 调节的肌动蛋白聚合从 TCR 开始。 TCR 中招募的分子调节肌动蛋白聚合，该过程驱动质膜运动和细胞扩散。
T cell receptor (TCR) engagement leads to actin polymerization at the site of T cell contact with antigen-presenting cells. Here we have studied the dynamic activity of proteins involved in regulating actin polymerization in live T cells after activation. Two such adaptor proteins, Nck and the Wiskott-Aldrich syndrome protein (WASp), were recruited to the TCR during initial T cell activation, where they colocalized with the tyrosine kinase Zap70. The recruitment of Nck and WASp depended on TCR-induced tyrosine phosphorylation and the LAT and SLP-76 adaptors. Nck and WASp migrated peripherally and accumulated at an actin-rich circumferential ring. Thus, actin polymerization regulated by the TCR begins at the TCR. Molecules recruited to the TCR regulate actin polymerization and this process drives plasma membrane movement and cellular spreading.