ArticleThe Journal of biological chemistry2014
Dissociated GαGTP and Gβγ protein subunits are the major activated form of heterotrimeric Gi/o proteins.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 33 citations in OpenAlex.
- Design of a metabolically-stable peptide therapeutic with triple-hormone-receptor agonist activity.Journal of computer-aided molecular design · 2026Article
- FLIPs: Genetically encoded molecular biosensors for functional imaging of cell signaling by linear dichroism microscopy.Science advances · 2026Article
- Heterotrimeric G proteins containing Gβ1γ2 subunits exhibit subtype-specific mobility differences in live cells.PloS one · 2026Article
- Characterization of the GTPγS release function of a G protein-coupled receptor.Nature communications · 2025Article
- Article
- Growth factor-dependent phosphorylation of GαScience signaling · 2024Article
- Serotonin 5-HTMolecular biology of the cell · 2023Article
- Every Detail Matters. That Is, How the Interaction between Gα Proteins and Membrane Affects Their Function.Membranes · 2021Review
- Quantitative linear dichroism imaging of molecular processes in living cells made simple by open software tools.Communications biology · 2021Article
- Inhibitory signaling in mammalian olfactory transduction potentially mediated by GαMolecular and cellular neurosciences · 2021Article
- Live cell optical assay for precise characterization of receptors coupling to Gα12.Basic & clinical pharmacology & toxicology · 2020Article
- Heterotrimeric GThe Journal of biological chemistry · 2020Review
- Targeting G protein-coupled receptor signaling at the G protein level with a selective nanobody inhibitor.Nature communications · 2018Article
- The G protein GThe Journal of biological chemistry · 2017Article
- A Quantitative Model of the GIRK1/2 Channel Reveals That Its Basal and Evoked Activities Are Controlled by Unequal Stoichiometry of Gα and Gβγ.PLoS computational biology · 2015Article
- Subcellular optogenetic inhibition of G proteins generates signaling gradients and cell migration.Molecular biology of the cell · 2014Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Although most heterotrimeric G proteins are thought to dissociate into Gα and Gβγ subunits upon activation, the evidence in the Gi/o family has long been inconsistent and contradictory. The Gi/o protein family mediates inhibition of cAMP production and regulates the activity of ion channels. On the basis of experimental evidence, both heterotrimer dissociation and rearrangement have been postulated as crucial steps of Gi/o protein activation and signal transduction. We have now investigated the process of Gi/o activation in living cells directly by two-photon polarization microscopy and indirectly by observations of G protein-coupled receptor kinase-derived polypeptides. Our observations of existing fluorescently labeled and non-modified Gαi/o constructs indicate that the molecular mechanism of Gαi/o activation is affected by the presence and localization of the fluorescent label. All investigated non-labeled, non-modified Gi/o complexes dissociate extensively upon activation. The dissociated subunits can activate downstream effectors and are thus likely to be the major activated Gi/o form. Constructs of Gαi/o subunits fluorescently labeled at the N terminus (GAP43-CFP-Gαi/o) seem to faithfully reproduce the behavior of the non-modified Gαi/o subunits. Gαi constructs labeled within the helical domain (Gαi-L91-YFP) largely do not dissociate upon activation, yet still activate downstream effectors, suggesting that the dissociation seen in non-modified Gαi/o proteins is not required for downstream signaling. Our results appear to reconcile disparate published data and settle a long running dispute.
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