Department of Pharmacology, Vanderbilt University, Nashville, TN 37232, USA.
Department of Pharmacology, Vanderbilt University, Nashville, TN 37232, USA.
Curr Opin Cell Biol. 2014 Apr;27:1-9. doi: 10.1016/j.ceb.2013.10.007. Epub 2013 Nov 16.
Among four vertebrate arrestins, only two are ubiquitously expressed. Arrestins specifically bind active phosphorylated G protein-coupled receptors (GPCRs), thereby precluding further G protein activation. Recent discoveries suggest that the formation of the arrestin-receptor complex initiates the second round of signaling with comparable biological importance. Despite having virtually no recognizable sequence motifs known to mediate protein-protein interactions, arrestins bind a surprising variety of signaling proteins with mind-boggling range of functional consequences. High conformational flexibility allows arrestins to show many distinct 'faces' to the world, which allows these relatively small ∼45kDa proteins to bind various partners under different physiological conditions, organizing multi-protein signaling complexes and localizing them to distinct subcellular compartments.
在四种脊椎动物 arrestin 中，只有两种广泛表达。arrestin 特异性结合活性磷酸化 G 蛋白偶联受体 (GPCR)，从而阻止进一步的 G 蛋白激活。最近的发现表明，arrestin-受体复合物的形成启动了第二轮具有相当重要生物学意义的信号转导。尽管 arrestin 没有任何已知的介导蛋白-蛋白相互作用的可识别序列基序，但它能与各种信号蛋白结合，具有令人惊讶的多样性，从而产生多种功能后果。高构象灵活性使 arrestin 能够向外界展示许多不同的“面孔”，这使得这些相对较小的约 45kDa 蛋白能够在不同的生理条件下与各种伴侣结合，形成多蛋白信号复合物，并将其定位到不同的亚细胞隔室。
