Griffiths Emily K, Penninger Josef M
Amgen, Department of Medical Biophysics, University of Toronto, 620 University Avenue, Toronto, Ontario, Canada M5G 2C1.
Sci STKE. 2002 Apr 9;2002(127):re3. doi: 10.1126/stke.2002.127.re3.
Adaptor proteins are essential components of T cell receptor (TCR) signaling cascades regulating gene transcription and cytoskeletal reorganization. The molecular adaptor adhesion- and degranulation-promoting adaptor protein (ADAP), also known as Fyn binding protein (FYB) or Slp-76-associated protein of 130 kilodaltons (SLAP-130), interacts with a number of signaling intermediates including Slp-76, the Src family tyrosine kinase Fyn, vasodilator-stimulated phosphoprotein (VASP), and the actin-nucleating protein WASP. Recently ADAP was shown genetically to positively regulate T cell activation, TCR-induced integrin clustering, and T cell adhesion. The mechanism by which ADAP couples TCR stimulation to integrin clustering remains unclear; however, studies of ADAP, the exchange factor Vav1, and WASP suggest that TCR and integrin clustering may be controlled by distinct signaling pathways.
衔接蛋白是调节基因转录和细胞骨架重组的T细胞受体（TCR）信号级联反应的重要组成部分。分子衔接蛋白——促进黏附和脱颗粒衔接蛋白（ADAP），也被称为Fyn结合蛋白（FYB）或130千道尔顿的Slp-76相关蛋白（SLAP-130），与许多信号中间体相互作用，包括Slp-76、Src家族酪氨酸激酶Fyn、血管舒张刺激磷蛋白（VASP）和肌动蛋白成核蛋白WASP。最近有研究表明，ADAP在基因层面上对T细胞活化、TCR诱导的整合素聚集和T细胞黏附起正向调节作用。ADAP将TCR刺激与整合素聚集联系起来的机制尚不清楚；然而，对ADAP、交换因子Vav1和WASP的研究表明，TCR和整合素聚集可能受不同信号通路的控制。
