Evidence map›Paper›PMID 32103024›Full record

ArticleNature communications2020

Structure of the G protein chaperone and guanine nucleotide exchange factor Ric-8A bound to Gαi1.

Levi J McClelland, Kaiming Zhang, Tung-Chung Mou, Jake Johnston, Cindee Yates-Hansen, Shanshan Li, Celestine J Thomas, Tzanko I Doukov, Sarah Triest, Alexandre Wohlkonig and 4 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.3field-weighted citation impact, top 20% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

18 citing papers in PubMed, 26 citations in OpenAlex.

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  18. Transducin Partners Outside the Phototransduction Pathway.Frontiers in cellular neuroscience · 2020
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

14 authors at 6 institutions in 2 countries.

Levi J McClelland *Center for Biomolecular Structure and Dynamics, University of Montana, Missoula, MT, 59812, USA.
Kaiming Zhang *Department of Bioengineering and James H. Clark Center, Stanford University, Stanford, CA, 94305, USA.ORCID http://orcid.org/0000-0003-0414-4776
Tung-Chung Mou *Center for Biomolecular Structure and Dynamics, University of Montana, Missoula, MT, 59812, USA.
Jake JohnstonCenter for Biomolecular Structure and Dynamics, University of Montana, Missoula, MT, 59812, USA.
Cindee Yates-HansenCenter for Biomolecular Structure and Dynamics, University of Montana, Missoula, MT, 59812, USA.
Shanshan LiDepartment of Bioengineering and James H. Clark Center, Stanford University, Stanford, CA, 94305, USA.ORCID http://orcid.org/0000-0002-7041-5960
Celestine J ThomasCenter for Biomolecular Structure and Dynamics, University of Montana, Missoula, MT, 59812, USA.
Tzanko I DoukovMacromolecular Crystallography Group, Stanford Synchrotron Radiation Light Source, SLAC National Accelerator Laboratory, Stanford University, Stanford, CA, 94025, USA.ORCID http://orcid.org/0000-0001-8625-2572
Sarah TriestStructural Biology Brussels, Vrije Universiteit Brussel (VUB), Brussels, Belgium.
Alexandre WohlkonigStructural Biology Brussels, Vrije Universiteit Brussel (VUB), Brussels, Belgium.
Gregory G TallDepartment of Pharmacology, University of Michigan Medical School, Ann Arbor, MI, 48109, USA.
Jan SteyaertStructural Biology Brussels, Vrije Universiteit Brussel (VUB), Brussels, Belgium.ORCID http://orcid.org/0000-0002-3825-874X
Wah ChiuDepartment of Bioengineering and James H. Clark Center, Stanford University, Stanford, CA, 94305, USA. wahc@stanford.edu.
Stephen R SprangCenter for Biomolecular Structure and Dynamics, University of Montana, Missoula, MT, 59812, USA. Stephen.sprang@umontana.edu.ORCID http://orcid.org/0000-0001-6307-6166
University of Montana · USVrije Universiteit Brussel · BESLAC National Accelerator Laboratory · USStanford University · USRegeneron (United States) · USUniversity of Michigan · US

Funding

X-ray Scattering Technology CoreP30GM133893 · NIGMS · BROOKHAVEN SCIENCE ASSOC-BROOKHAVEN LAB · PI Sean McSweeney · 2019 to 2026
$38.6M
X-ray Absorption Spectroscopy (XAS) pp.711-759P41GM103393 · NIGMS · STANFORD UNIVERSITY · PI HODGSON, KEITH O · 2012 to 2019
$30.6M
Surveillance genome sequencing to detect SARS-CoV-2 virus variants in MontanaP20GM103546 · NIGMS · UNIVERSITY OF MONTANA · PI BOWLER, BRUCE E · 2012 to 2021
$19.2M
Life Science and Biomedical technology Research center at NSLS-II LSBRP41GM111244 · NIGMS · BROOKHAVEN SCIENCE ASSOC-BROOKHAVEN LAB · PI MCSWEENEY, SEAN · 2014 to 2018
$16.4M
3 D ELECTRON MICROSCOPY OF MACROMOLECULES (5P41RR002250-27)P41GM103832 · NIGMS · STANFORD UNIVERSITY · PI CHIU, WAH · 2012 to 2019
$15.1M
Time resolved SAXS studies on the RP2/Arl3 complex pp.484-485P41GM103622 · NIGMS · ILLINOIS INSTITUTE OF TECHNOLOGY · PI IRVING, THOMAS C · 2012 to 2020
$11.9M
Unified Data Resource for Large Complexes Determined by Cryo-Electron MicroscopyR01GM079429 · NIGMS · STANFORD UNIVERSITY · PI CHIU, WAH · 2007 to 2021
$11.6M
Regulation of Heterotrimeric G proteins by non-receptor activatorsR01GM088242 · NIGMS · UNIVERSITY OF ROCHESTER · PI TALL, GREGORY GORDON · 2009 to 2022
$4.2M
Mechanism of G protein Activation by Ric-8A - competitive revision of R01GM105993R01GM105993 · NIGMS · UNIVERSITY OF MONTANA · PI SPRANG, STEPHEN R · 2013 to 2020
$2.8M
Acquisition of a 300 kV Electron Microscope for Structural BiologyS10OD021600 · OD · STANFORD UNIVERSITY · PI CHIU, WAH · 2016 to 2016
$2.0M
Advanced Pixel Array Detector for Time-Resolved SAXS and Fiber DiffractionS10OD018090 · OD · ILLINOIS INSTITUTE OF TECHNOLOGY · PI IRVING, THOMAS C · 2014 to 2014
$529k
NIGMS NIH HHS P20 GM103546NIGMS NIH HHS P30 GM133893NIGMS NIH HHS P41 GM103393NIGMS NIH HHS P41 GM103622NIGMS NIH HHS P41 GM103832NIGMS NIH HHS P41 GM111244NIGMS NIH HHS R01 GM079429NIGMS NIH HHS R01 GM088242NIGMS NIH HHS R01 GM105993NIH HHS S10 OD018090NIH HHS S10 OD021600
6 · The paper itself

Abstract

Ric-8A is a cytosolic Guanine Nucleotide exchange Factor (GEF) that activates heterotrimeric G protein alpha subunits (Gα) and serves as an essential Gα chaperone. Mechanisms by which Ric-8A catalyzes these activities, which are stimulated by Casein Kinase II phosphorylation, are unknown. We report the structure of the nanobody-stabilized complex of nucleotide-free Gα bound to phosphorylated Ric-8A at near atomic resolution by cryo-electron microscopy and X-ray crystallography. The mechanism of Ric-8A GEF activity differs considerably from that employed by G protein-coupled receptors at the plasma membrane. Ric-8A engages a specific conformation of Gα at multiple interfaces to form a complex that is stabilized by phosphorylation within a Ric-8A segment that connects two Gα binding sites. The C-terminus of Gα is ejected from its beta sheet core, thereby dismantling the GDP binding site. Ric-8A binds to the exposed Gα beta sheet and switch II to stabilize the nucleotide-free state of Gα.

Indexed as

AnimalsAsymmetric Cell DivisionBinding SitesCamelids, New WorldCasein Kinase IICell MembraneCryoelectron MicroscopyCrystallography, X-RayEmbryonic DevelopmentGTP-Binding Protein alpha SubunitsGuanine Nucleotide Exchange FactorsMolecular ChaperonesMultiprotein ComplexesPhosphorylationProtein BindingProtein ConformationCasein Kinase IIGTP-Binding Protein alpha SubunitsGuanine Nucleotide Exchange FactorsMolecular ChaperonesMultiprotein Complexes

Identifiers

PMID32103024
PMCPMC7044438
OpenAlexW3008041610

What OpenQuestion holds

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Registered trials

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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.