Peterson E J, Woods M L, Dmowski S A, Derimanov G, Jordan M S, Wu J N, Myung P S, Liu Q H, Pribila J T, Freedman B D, Shimizu Y, Koretzky G A
The Abramson Family Cancer Research Institute, Department of Medicine, School of Medicine, University of Pennsylvania, Philadelphia, PA, 19104, USA.
Science. 2001 Sep 21;293(5538):2263-5. doi: 10.1126/science.1063486.
SLAP-130/Fyb (SLP-76-associated phosphoprotein or Fyn-binding protein; also known as Fyb/Slap) is a hematopoietic-specific adapter, which associates with and modulates function of SH2-containing leukocyte phosphoprotein of 76 kilodaltons (SLP-76). T cells from mice lacking SLAP-130/Fyb show markedly impaired proliferation following CD3 engagement. In addition, the T cell receptor (TCR) in SLAP-130/Fyb mutant cells fails to enhance integrin-dependent adhesion. Although TCR-induced actin polymerization is normal, TCR-stimulated clustering of the integrin LFA-1 is defective in SLAP-130/Fyb-deficient cells. These data indicate that SLAP-130/Fyb is important for coupling TCR-mediated actin cytoskeletal rearrangement with activation of integrin function, and for T cells to respond fully to activating signals.
SLAP-130/Fyb（与SLP-76相关的磷蛋白或Fyn结合蛋白；也称为Fyb/Slap）是一种造血特异性衔接蛋白，它与76千道尔顿含SH2的白细胞磷蛋白（SLP-76）结合并调节其功能。缺乏SLAP-130/Fyb的小鼠的T细胞在CD3参与后增殖明显受损。此外，SLAP-130/Fyb突变细胞中的T细胞受体（TCR）未能增强整合素依赖性黏附。尽管TCR诱导的肌动蛋白聚合正常，但在缺乏SLAP-130/Fyb的细胞中，TCR刺激的整合素LFA-1聚集存在缺陷。这些数据表明，SLAP-130/Fyb对于将TCR介导的肌动蛋白细胞骨架重排与整合素功能激活相偶联以及T细胞对激活信号做出充分反应很重要。
