Integrin structures and conformational signaling
Integrin structures and conformational signaling
复制标题
DOI：
10.1016/j.ceb.2006.08.005
复制
发表时间：
2006-10-01
影响因子：
7.5
通讯作者：
Springer, Timothy A.
中科院分区：
文献类型：
--
作者：
Luo, Bing-Hao;Springer, Timothy A.
整合素是细胞粘附分子，在发育、伤口愈合、止血、免疫和癌症中发挥着关键作用。过去两年的进展揭示了整合素调控和信号传导的结构基础，特别是弯曲构象和延伸构象之间的整体构象变化如何与调节配体亲和力的域间和域内形状转变相关。 α 1 和 β 1 结构域 C 端螺旋的向下运动以及混合结构域的摆动在整联蛋白构象信号传导中发挥着关键作用。实验还表明，整合素通过将细胞外构象变化与α和β跨膜和细胞质结构域的解扣和分离结合起来，跨质膜传递双向信号。
Integrins are cell adhesion molecules that play critical roles in development, wound healing, hemostasis, immunity and cancer. Advances in the past two years have shed light on the structural basis for integrin regulation and signaling, especially on how global conformational changes between bent and extended conformations relate to the inter-domain and intra-domain shape shifting that regulates affinity for ligand. The downward movements of the C-terminal helices of the alpha 1 and beta 1 domains and the swing-out of the hybrid domain play pivotal roles in integrin conformational signaling. Experiments have also shown that integrins transmit bidirectional signals across the plasma membrane by coupling extracellular conformational change with an unclasping and separation of the alpha and beta transmembrane and cytoplasmic domains.