| Title: |
Noncanonical scaffolding of G αi and β-arrestin by G protein–coupled receptors |
| Authors: |
Smith, Jeffrey S.; Pack, Thomas F.; Inoue, Asuka; Lee, Claudia; Zheng, Kevin; Choi, Issac; Eiger, Dylan S.; Warman, Anmol; Xiong, Xinyu; Ma, Zhiyuan; Viswanathan, Gayathri; Levitan, Ian M.; Rochelle, Lauren K.; Staus, Dean P.; Snyder, Joshua C.; Kahsai, Alem W.; Caron, Marc G.; Rajagopal, Sudarshan |
| Contributors: |
National Institute of Mental Health; National Institute on Drug Abuse; National Heart, Lung, and Blood Institute; National Institute of General Medical Sciences |
| Source: |
Science ; volume 371, issue 6534 ; ISSN 0036-8075 1095-9203 |
| Publisher Information: |
American Association for the Advancement of Science (AAAS) |
| Publication Year: |
2021 |
| Description: |
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 |
| Document Type: |
article in journal/newspaper |
| Language: |
English |
| DOI: |
10.1126/science.aay1833 |
| Availability: |
https://doi.org/10.1126/science.aay1833; https://syndication.highwire.org/content/doi/10.1126/science.aay1833; https://www.science.org/doi/pdf/10.1126/science.aay1833 |
| Accession Number: |
edsbas.E9A671EF |
| Database: |
BASE |