Ménasché Gaël, Kliche Stefanie, Bezman Natalie, Schraven Burkhart
Abramson Family Cancer Research Institute, University of Pennsylvania School of Medicine, Philadelphia, PA, USA.
Immunol Rev. 2007 Aug;218:82-91. doi: 10.1111/j.1600-065X.2007.00543.x.
Integrins are critical for the migration of T cells to lymphoid organs and to sites of inflammation and are also necessary for productive interactions between T cells and antigen-presenting cells. Integrin activation is enhanced following T-cell receptor (TCR) engagement, as signals initiated by the TCR increase affinity and avidity of integrins for their ligands. This process, known as inside-out signaling, has been shown to require several molecular components including the cytosolic adapter proteins adhesion and degranulation-promoting adapter protein and Src homology 2 domain-containing adapter protein of 55 kDa, the low molecular weight guanosine triphosphatase Rap1, and the Rap1 effector proteins Rap1 guanosine triphosphate-interacting adapter molecule, regulator of adhesion and cell polarization enriched in lymphoid tissues, and protein kinase D1. Herein, we review recent findings about how the TCR is linked to integrin activation through inside-out signaling.
整合素对于T细胞迁移至淋巴器官和炎症部位至关重要，也是T细胞与抗原呈递细胞之间有效相互作用所必需的。T细胞受体（TCR）激活后，整合素激活增强，因为TCR引发的信号增加了整合素对其配体的亲和力和avidity。这个过程，称为外向内信号传导，已被证明需要几种分子成分，包括胞质衔接蛋白黏附与脱颗粒促进衔接蛋白和55 kDa含Src同源2结构域的衔接蛋白、低分子量鸟苷三磷酸酶Rap1以及Rap1效应蛋白Rap1鸟苷三磷酸相互作用衔接分子、富含淋巴组织的黏附与细胞极化调节剂和蛋白激酶D1。在此，我们综述了关于TCR如何通过外向内信号传导与整合素激活相联系的最新发现。
