Fu Guanyuan, Wang Wei, Luo Bing-Hao
Department of Biological Sciences, Louisiana State University, Baton Rouge, LA, USA.
Methods Mol Biol. 2012;757:81-99. doi: 10.1007/978-1-61779-166-6_7.
Integrins are cell adhesion molecules that play important roles in many biological processes including hemostasis, immune responses, development, and cancer. Their adhesiveness is dynamically regulated through a process termed inside-out signaling. In addition, ligand binding transduces outside-in signals from the extracellular domain to the cytoplasm. Advances in the past several years have shed light on structural basis for integrin regulation and signaling, especially how the large-scale reorientations of the ectodomain are related to the inter-domain and intra-domain shape shifting that changes ligand-binding affinity. Experiments have also shown how the conformational changes of the ectodomain are linked to changes in the α- and β-subunit transmembrane and cytoplasmic domains.
整合素是细胞粘附分子，在包括止血、免疫反应、发育和癌症在内的许多生物学过程中发挥重要作用。它们的粘附性通过一种称为外向内信号传导的过程进行动态调节。此外，配体结合将从细胞外结构域到细胞质的由外向内信号进行转导。过去几年的进展揭示了整合素调节和信号传导的结构基础，特别是胞外结构域的大规模重新定向如何与改变配体结合亲和力的结构域间和结构域内的形状变化相关。实验还表明了胞外结构域的构象变化如何与α和β亚基跨膜及胞质结构域的变化相联系。
