ArticleeLife2019
Cryo-EM structure of the rhodopsin-Gαi-βγ complex reveals binding of the rhodopsin C-terminal tail to the gβ subunit.
Article in eLife, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
32 citing papers in PubMed, 73 citations in OpenAlex.
- Tool antibody fragments reveal multiple conformations of the rhodopsin-Gi signaling complex.Biophysical journal · 2026Article
- Structural determinants of G protein subtype selectivity at the serotonin receptor 5-HT1A.Science advances · 2025Article
- Deprotonation of retinal Schiff base and structural dynamics in the early photoreaction of primate blue cone visual pigment.Biophysical journal · 2025Article
- Signal termination of the chemokine receptor CCR9 is governed by an arrestin-independent phosphorylation mechanism.The Journal of biological chemistry · 2025Article
- Exploring a Novel Hypothesis: Could the Eye Function as a Radar or Ultrasound Device in Depth and Distance Perception? Neurophysiological Insights.Life (Basel, Switzerland) · 2025Article
- Mechanisms of Rhodopsin-Related Inherited Retinal Degeneration and Pharmacological Treatment Strategies.Cells · 2025Review
- Active state structures of a bistable visual opsin bound to G proteins.Nature communications · 2024Article
- Control of G protein-coupled receptor function via membrane-interacting intrinsically disordered C-terminal domains.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Bayesian network models identify cooperative GPCR:G protein interactions that contribute to G protein coupling.The Journal of biological chemistry · 2024Article
- Control of G protein-coupled receptor function via membrane-interacting intrinsically disordered C-terminal domains.bioRxiv : the preprint server for biology · 2024Article
- Bayesian network models identify co-operative GPCR:G protein interactions that contribute to G protein coupling.bioRxiv : the preprint server for biology · 2023Article
- Beyond the G protein α subunit: investigating the functional impact of other components of the GαiCell communication and signaling : CCS · 2023Article
- Structural insights into ligand recognition and activation of the medium-chain fatty acid-sensing receptor GPR84.Nature communications · 2023Article
- Article
- Two-step structural changes in M3 muscarinic receptor activation rely on the coupled GNature communications · 2023Article
- Correction of rhodopsin serial crystallography diffraction intensities for a lattice-translocation defect.Acta crystallographica. Section D, Structural biology · 2023Article
- Functional optimization of light-activatable Opto-GPCRs: Illuminating the importance of the proximal C-terminus in G-protein specificity.Frontiers in cell and developmental biology · 2023Article
- Dynamic spatiotemporal determinants modulate GPCR:G protein coupling selectivity and promiscuity.Nature communications · 2022Article
- A model for how Gβγ couples Gα to GPCR.The Journal of general physiology · 2022Article
- G protein-coupled receptor-effector macromolecular membrane assemblies (GEMMAs).Pharmacology & therapeutics · 2022Review
Corrections and comments
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Authors and funding
14 authors at 4 institutions in 3 countries.
Funding
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.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.