Distinct conformations of GPCR-β-arrestin complexes mediate desensitization, signaling, and endocytosis.

@article{Cahill2017DistinctCO,
  title={Distinct conformations of GPCR-β-arrestin complexes mediate desensitization, signaling, and endocytosis.},
  author={Thomas Joseph Cahill and Alex R. B. Thomsen and Jeffrey Tarrasch and Bianca Plouffe and Anthony Nguyen and Fan Yang and Li-Yin Huang and Alem W. Kahsai and Daniel L Bassoni and Bryant J Gavino and Jane E. Lamerdin and Sarah Triest and Arun Kumar Shukla and Benjamin Berger and J. Russell Little and Albert Antar and Adi Blanc and Chang-Xiu Qu and Xin Mao Chen and Kouki Kawakami and Asuka Inoue and Junken Aoki and Jan Steyaert and Jin-peng Sun and Michel Bouvier and Georgios Skiniotis and Robert J Lefkowitz},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2017},
  volume={114 10},
  pages={2562-2567}
}
β-Arrestins (βarrs) interact with G protein-coupled receptors (GPCRs) to desensitize G protein signaling, to initiate signaling on their own, and to mediate receptor endocytosis. Prior structural studies have revealed two unique conformations of GPCR-βarr complexes: the "tail" conformation, with βarr primarily coupled to the phosphorylated GPCR C-terminal tail, and the "core" conformation, where, in addition to the phosphorylated C-terminal tail, βarr is further engaged with the receptor… CONTINUE READING