1. Noncanonical scaffolding of G αi and β-arrestin by G protein–coupled receptors
- Author
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Claudia Lee, Jeffrey S. Smith, Dean P. Staus, Sudarshan Rajagopal, Thomas F. Pack, Issac Choi, Xinyu Xiong, Zhiyuan Ma, Dylan Eiger, Ian M. Levitan, Gayathri Viswanathan, Alem W. Kahsai, Kevin Zheng, Joshua C. Snyder, Marc G. Caron, Anmol Warman, Asuka Inoue, and Lauren K. Rochelle
- Subjects
Multidisciplinary ,Chemistry ,G protein ,GTP-Binding Protein alpha Subunits ,Heterotrimeric G protein ,Gi alpha subunit ,Arrestin ,Signal transducing adaptor protein ,Signal transduction ,G protein-coupled receptor ,Cell biology - Abstract
Another way for GPCRs to signal G protein–coupled receptors (GPCRs) normally transmit signals by coupling to heterotrimeric guanine nucleotide–binding proteins (G proteins) or by binding β-arrestin proteins. Smith et al. provide evidence for another mechanism, an approximate combination of the two. They monitored the interaction of vasopressin type 2 receptors (V2Rs) and G α proteins in cultured cells using bioluminescent resonance energy transfer. Even though V2Rs do not signal canonically through G α i proteins, they promoted the formation of complexes containing β-arrestin and G α i , and this led to downstream signaling to extracellular signal-regulated kinase protein kinases. Science , this issue p. eaay1833
- Published
- 2021
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