Tesmer John J G
Life Sciences Institute and Departments of Pharmacology and Biological Chemistry, University of Michigan, Ann Arbor, Michigan 48109-2216, USA.
Nat Rev Mol Cell Biol. 2016 Jul;17(7):439-50. doi: 10.1038/nrm.2016.36. Epub 2016 Apr 20.
A revolution in the analysis of seven transmembrane domain (7TM) receptors has provided detailed information about how these physiologically important signalling proteins interact with extracellular cues. However, it has proved much more challenging to understand how 7TM receptors convey information to their principal intracellular targets: heterotrimeric G proteins, G protein-coupled receptor kinases and arrestins. Recent structures now suggest a common mechanism that enables these structurally diverse cytoplasmic proteins to 'hitch a ride' on hundreds of different activated 7TM receptors in order to instigate physiological change.
七跨膜结构域(7TM)受体分析领域的一场革命,为这些具有重要生理功能的信号蛋白如何与细胞外信号相互作用提供了详细信息。然而,要理解7TM受体如何将信息传递给其主要的细胞内靶点,即异源三聚体G蛋白、G蛋白偶联受体激酶和抑制蛋白,却困难得多。最近的结构研究表明,存在一种共同机制,使这些结构各异的胞质蛋白能够“搭乘”数百种不同的活化7TM受体,从而引发生理变化。