ADAP-ting TCR signaling to integrins.
ADAP-ting TCR signaling to integrins.
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DOI：
10.1126/stke.2002.127.re3
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发表时间：
2002-04-09
期刊：
影响因子：
--
通讯作者：
Penninger, Josef M
中科院分区：
文献类型：
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作者：
Griffiths, Emily K;Penninger, Josef M
衔接子蛋白是T细胞受体（TCR）信号级联的重要组成部分，调节基因转录和细胞骨架重组。分子衔接子粘附和脱颗粒促进衔接子蛋白（ADAP），也称为Fyn结合蛋白（FYB）或130千道尔顿的Slp-76相关蛋白（Srp-130），与许多信号传导中间体相互作用，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，ADAP被证明在遗传上正调节T细胞活化、TCR诱导的整合素聚集和T细胞粘附。ADAP将TCR刺激与整联蛋白聚集偶联的机制尚不清楚;然而，对ADAP、交换因子Vav 1和WASP的研究表明，TCR和整联蛋白聚集可能受不同的信号通路控制。
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.