Department of Medicine, Duke University Medical Center, Durham, NC 27710, USA.
Trends Biochem Sci. 2011 Sep;36(9):457-69. doi: 10.1016/j.tibs.2011.06.003. Epub 2011 Jul 20.
β-Arrestins, originally discovered to desensitize activated seven transmembrane receptors (7TMRs; also known as G-protein-coupled receptors, GPCRs), are now well established mediators of receptor endocytosis, ubiquitylation and G protein-independent signaling. Recent global analyses of β-arrestin interactions and β-arrestin-dependent phosphorylation events have uncovered several previously unanticipated roles of β-arrestins in a range of cellular signaling events. These findings strongly suggest that the functional roles of β-arrestins are much broader than currently understood. Biophysical studies aimed at understanding multiple active conformations of the 7TMRs and the β-arrestins have begun to unravel the mechanistic basis for the diverse functional capabilities of β-arrestins in cellular signaling.
β-arrestins，最初被发现可使激活的七跨膜受体（7TMRs；也称为 G 蛋白偶联受体，GPCRs）脱敏，现在已被很好地确认为受体内化、泛素化和 G 蛋白非依赖性信号转导的介质。最近对β-arrestin 相互作用和β-arrestin 依赖性磷酸化事件的全球分析揭示了β-arrestin 在一系列细胞信号事件中以前未预料到的作用。这些发现强烈表明，β-arrestin 的功能作用比目前所理解的要广泛得多。旨在了解 7TMRs 和β-arrestin 的多种活性构象的生物物理研究已开始揭示β-arrestin 在细胞信号转导中具有多种功能能力的机制基础。
