Department of Biochemistry and Molecular Biology, Thomas Jefferson University, Philadelphia, PA 19107, USA.
Department of Biochemistry and Molecular Biology, Thomas Jefferson University, Philadelphia, PA 19107, USA.
Curr Opin Cell Biol. 2014 Apr;27:63-71. doi: 10.1016/j.ceb.2013.11.005. Epub 2013 Dec 14.
The arrestin clan can now be broadly divided into three structurally similar subgroups: the originally identified arrestins (visual and β-arrestins), the α-arrestins and a group of Vps26-related proteins. The visual and β-arrestins selectively bind to agonist-occupied phosphorylated G protein-coupled receptors (GPCRs) and inhibit GPCR coupling to heterotrimeric G proteins while the β-arrestins also function as adaptor proteins to regulate GPCR trafficking and G protein-independent signaling. The α-arrestins have also recently been implicated in regulating GPCR trafficking while Vps26 regulates retrograde trafficking. In this review, we provide an overview of the α-arrestins and β-arrestins with a focus on our current understanding of how these adaptor proteins regulate GPCR trafficking.
现在可以将 arrestin 家族大致分为三个结构相似的亚群：最初确定的 arrestin（视觉和β-arrestin）、α-arrestin 和一组与 Vps26 相关的蛋白质。视觉和β-arrestin 选择性地结合到激动剂占据的磷酸化 G 蛋白偶联受体 (GPCR) 上，并抑制 GPCR 与异三聚体 G 蛋白的偶联，而β-arrestin 还作为衔接蛋白来调节 GPCR 运输和 G 蛋白独立信号转导。最近，α-arrestin 也被牵涉到调节 GPCR 运输，而 Vps26 调节逆行运输。在这篇综述中，我们提供了α-arrestin 和 β-arrestin 的概述，重点介绍了这些衔接蛋白如何调节 GPCR 运输。
