Cryo-EM structure of the rhodopsin-Gαi-βγ complex reveals binding of the rhodopsin C-terminal tail to the gβ subunit

Open access
Date
2019-06-28Type
- Journal Article
Citations
Cited 28 times in
Web of Science
Cited 33 times in
Scopus
ETH Bibliography
yes
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Abstract
One of the largest membrane protein families in eukaryotes are G protein-coupled receptors (GPCRs). GPCRs modulate cell physiology by activating diverse intracellular transducers, prominently heterotrimeric G proteins. The recent surge in structural data has expanded our understanding of GPCR-mediated signal transduction. However, many aspects, including the existence of transient interactions, remain elusive. We present the cryo-EM structure of the light-sensitive GPCR rhodopsin in complex with heterotrimeric Gi. Our density map reveals the receptor C-terminal tail bound to the Gβ subunit of the G protein, providing a structural foundation for the role of the C-terminal tail in GPCR signaling, and of Gβ as scaffold for recruiting Gα subunits and G protein-receptor kinases. By comparing available complexes, we found a small set of common anchoring points that are G protein-subtype specific. Taken together, our structure and analysis provide new structural basis for the molecular events of the GPCR signaling pathway. Show more
Permanent link
https://doi.org/10.3929/ethz-b-000355900Publication status
publishedExternal links
Journal / series
eLifeVolume
Pages / Article No.
Publisher
eLife Sciences Publications Ltd.Funding
160805 - Targeting Cancer Cells with Hybrid and Heterovalent Ligands at Controlled Distances (SNF)
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Show all metadata
Citations
Cited 28 times in
Web of Science
Cited 33 times in
Scopus
ETH Bibliography
yes
Altmetrics