ArticleCellular signalling2009
The c-terminus of GRK3 indicates rapid dissociation of G protein heterotrimers.
Article in Cellular signalling, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 128 papers.
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Who cites it
128 citing papers in PubMed.
- Dual-target mu opioid-dopamine DEuropean journal of medicinal chemistry · 2026Article
- G protein diffusion states reveal receptor binding dynamics at single-molecule scale.Cell chemical biology · 2026Article
- Inhibitory probes for spatiotemporal analysis of GαNature chemical biology · 2026Article
- The structure of the dopamine DScience advances · 2026Article
- G protein signaling capabilities at the bradykinin 2 receptor.Naunyn-Schmiedeberg's archives of pharmacology · 2026Article
- Chemokine receptor activity is differentially regulated by membrane cholesterol.bioRxiv : the preprint server for biology · 2026Article
- G-protein regulatory network governs receptor internalization dynamics.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Genome editing-based refinement of GPCR visualization in mice using the oxytocin receptor as a model.Scientific reports · 2026Article
- RGS proteins: Potential regulators of mouse melanopsin's signaling phototransduction cascade across ipRGC subtypes.Biophysical journal · 2026Article
- FLIPs: Genetically encoded molecular biosensors for functional imaging of cell signaling by linear dichroism microscopy.Science advances · 2026Article
- Metabotropic glutamate receptor homo- and heterodimers exhibit distinct responses to orthosteric and allosteric ligands.Molecular pharmacology · 2025Article
- GNature communications · 2025Article
- Arrestin-independent internalization of the GLP-1 receptor is facilitated by a GRK, clathrin, and caveolae-dependent mechanism.The FEBS journal · 2025Article
- A sensitive biosensor of endogenous GαScience signaling · 2025Article
- The structure and function of the ghrelin receptor coding for drug actions.Nature structural & molecular biology · 2025Article
- N-terminal fragment shedding contributes to signaling of the full-length adhesion receptor ADGRL3.The Journal of biological chemistry · 2025Article
- Quantitative approaches for studying G protein-coupled receptor signalling and pharmacology.Journal of cell science · 2025Review
- Protocol to investigate G protein-coupled receptor signaling kinetics and concentration-dependent responses using ONE-GO biosensors.STAR protocols · 2024Article
- Essential strategies for the detection of constitutive and ligand-dependent Gi-directed activity of 7TM receptors using bioluminescence resonance energy transfer.bioRxiv : the preprint server for biology · 2024Article
- Article
68 more citing papers are in PubMed but not listed here.
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Authors and funding
4 authors.
Funding
Abstract
Signals mediated by heterotrimeric G proteins often develop over the course of tens of milliseconds, and could require either conformational rearrangement or complete physical dissociation of Galphabetagamma heterotrimers. Although it is known that some active heterotrimers are dissociated (into Galpha and Gbetagamma) at steady-state, it is not clear that dissociation occurs quickly enough to participate in rapid signaling. Here we show that fusion proteins containing the c-terminus of GPCR kinase 3 (GRK3ct) and either the fluorescent protein cerulean or Renilla luciferase bind to venus-labeled Gbetagamma dimers (Gbetagamma-V), resulting in Förster or bioluminescence resonance energy transfer (FRET or BRET). GRK3ct fusion proteins are freely-diffusible, and do not form preassembled complexes with G proteins. GRK3ct fusion proteins bind to free Gbetagamma-V dimers but not to rearranged heterotrimers, and thus can report G protein dissociation with high temporal resolution. We find that heterotrimer dissociation can occur in living cells in less than 100 ms. Under the conditions of these experiments diffusion and collision of masGRK3ct fusion proteins and Gbetagamma-V were not rate-limiting. These results indicate that G protein heterotrimers can dissociate quickly enough to participate in rapid signaling.
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