Department of Pharmacology, Yale University School of Medicine, New Haven, CT 06520, United States of America.
Department of Pharmacology, Yale University School of Medicine, New Haven, CT 06520, United States of America; Department of Cell Biology, Yale University School of Medicine, New Haven, CT 06520, United States of America..
Biochim Biophys Acta Biomembr. 2020 May 1;1862(5):183206. doi: 10.1016/j.bbamem.2020.183206. Epub 2020 Jan 25.
The integrin family of transmembrane adhesion receptors is essential for sensing and adhering to the extracellular environment. Integrins are heterodimers composed of non-covalently associated α and β subunits that engage extracellular matrix proteins and couple to intracellular signaling and cytoskeletal complexes. Humans have 24 different integrin heterodimers with differing ligand binding specificities and non-redundant functions. Complex structural rearrangements control the ability of integrins to engage ligands and to activate diverse downstream signaling networks, modulating cell adhesion and dynamics, processes which are crucial for metazoan life and development. Here we review the structural and signaling functions of integrins focusing on recent advances which have enhanced our understanding of how integrins are activated and regulated, and the cytoplasmic signaling networks downstream of integrins.
整联蛋白家族是细胞表面的黏附受体，对于感知和黏附细胞外环境至关重要。整联蛋白是由非共价连接的α和β亚基组成的异二聚体，可与细胞外基质蛋白结合，并与细胞内信号和细胞骨架复合物偶联。人类有 24 种不同的整联蛋白异二聚体，具有不同的配体结合特异性和非冗余功能。复杂的结构重排控制着整联蛋白与配体结合和激活不同下游信号网络的能力，调节细胞黏附和动力学，这些过程对于后生动物的生命和发育至关重要。在这里，我们回顾了整联蛋白的结构和信号功能，重点介绍了最近的进展，这些进展增强了我们对整联蛋白如何被激活和调节以及整联蛋白下游的细胞质信号网络的理解。
