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使T细胞受体信号适应整合素

ADAP-ting TCR signaling to integrins.

作者信息

Griffiths Emily K, Penninger Josef M

机构信息

Amgen, Department of Medical Biophysics, University of Toronto, 620 University Avenue, Toronto, Ontario, Canada M5G 2C1.

出版信息

Sci STKE. 2002 Apr 9;2002(127):re3. doi: 10.1126/stke.2002.127.re3.

Abstract

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.

摘要

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。

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