ArticleeLife2016
Ric-8A, a G protein chaperone with nucleotide exchange activity induces long-range secondary structure changes in Gα.
Article in eLife, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
20 citing papers in PubMed, 29 citations in OpenAlex.
- Article
- Unisexual reproduction in the global human fungal pathogenProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Unisexual reproduction in the global human fungal pathogenbioRxiv : the preprint server for biology · 2025Article
- Influence of expression and purification protocols on Gα biochemical activity: kinetics of plant and mammalian G protein cycles.Frontiers in molecular biosciences · 2025Article
- Article
- The G protein alpha chaperone and guanine-nucleotide exchange factor RIC-8 regulates cilia morphogenesis in Caenorhabditis elegans sensory neurons.PLoS genetics · 2023Article
- Structures of Ric-8B in complex with Gα protein folding clients reveal isoform specificity mechanisms.Structure (London, England : 1993) · 2023Article
- Anti-CRISPR proteins function through thermodynamic tuning and allosteric regulation of CRISPR RNA-guided surveillance complex.Nucleic acids research · 2022Article
- Review
- Spindle positioning and its impact on vertebrate tissue architecture and cell fate.Nature reviews. Molecular cell biology · 2021Review
- Ric-8A, a GEF, and a Chaperone for G Protein α-Subunits: Evidence for the Two-Faced Interface.BioEssays : news and reviews in molecular, cellular and developmental biology · 2020Article
- Do All Roads Lead to Rome in G-Protein Activation?Trends in biochemical sciences · 2020Review
- Structure of the G protein chaperone and guanine nucleotide exchange factor Ric-8A bound to Gαi1.Nature communications · 2020Article
- Large-scale conformational rearrangement of the α5-helix of Gα subunits in complex with the guanine nucleotide exchange factor Ric8A.The Journal of biological chemistry · 2019Article
- Genome-wide CRISPR screening reveals genetic modifiers of mutant EGFR dependence in human NSCLC.eLife · 2019Article
- Structural basis for GPCR-independent activation of heterotrimeric Gi proteins.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Structural underpinnings of Ric8A function as a G-protein α-subunit chaperone and guanine-nucleotide exchange factor.Nature communications · 2019Article
- Structure, Function, and Dynamics of the Gα Binding Domain of Ric-8A.Structure (London, England : 1993) · 2019Article
- Article
- Dual phosphorylation of Ric-8A enhances its ability to mediate G protein α subunit folding and to stimulate guanine nucleotide exchange.Science signaling · 2018Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Cytosolic Ric-8A has guanine nucleotide exchange factor (GEF) activity and is a chaperone for several classes of heterotrimeric G protein α subunits in vertebrates. Using Hydrogen-Deuterium Exchange-Mass Spectrometry (HDX-MS) we show that Ric-8A disrupts the secondary structure of the Gα Ras-like domain that girds the guanine nucleotide-binding site, and destabilizes the interface between the Gαi1 Ras and helical domains, allowing domain separation and nucleotide release. These changes are largely reversed upon binding GTP and dissociation of Ric-8A. HDX-MS identifies a potential Gα interaction site in Ric-8A. Alanine scanning reveals residues crucial for GEF activity within that sequence. HDX confirms that, like G protein-coupled receptors (GPCRs), Ric-8A binds the C-terminus of Gα. In contrast to GPCRs, Ric-8A interacts with Switches I and II of Gα and possibly at the Gα domain interface. These extensive interactions provide both allosteric and direct catalysis of GDP unbinding and release and GTP binding.
Indexed as
Identifiers
What OpenQuestion holds
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.