Evidence map›Paper›PMID 27022092›Full record

ArticleThe Journal of cell biology2016

G3BP-Caprin1-USP10 complexes mediate stress granule condensation and associate with 40S subunits.

Nancy Kedersha, Marc D Panas, Christopher A Achorn, Shawn Lyons, Sarah Tisdale, Tyler Hickman, Marshall Thomas, Judy Lieberman, Gerald M McInerney, Pavel Ivanov and 1 more

Erratum issuedAbstract readVideo-Audio Media
In one paragraph

Article in The Journal of cell biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 423 papers.

0numbers the graph read from it
0cells of the map it votes in
423citing papers in PubMed
–field-weighted citation impact
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

423 citing papers in PubMed.

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363 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

11 authors.

Nancy KedershaDivision of Rheumatology, Immunology and Allergy, Harvard Medical School and Brigham and Women's Hospital, Boston, MA 02115 nkedersha@rics.bwh.harvard.edu.
Marc D PanasDivision of Rheumatology, Immunology and Allergy, Harvard Medical School and Brigham and Women's Hospital, Boston, MA 02115.
Christopher A AchornDivision of Rheumatology, Immunology and Allergy, Harvard Medical School and Brigham and Women's Hospital, Boston, MA 02115.
Shawn LyonsDivision of Rheumatology, Immunology and Allergy, Harvard Medical School and Brigham and Women's Hospital, Boston, MA 02115.
Sarah TisdaleDivision of Rheumatology, Immunology and Allergy, Harvard Medical School and Brigham and Women's Hospital, Boston, MA 02115.
Tyler HickmanDivision of Rheumatology, Immunology and Allergy, Harvard Medical School and Brigham and Women's Hospital, Boston, MA 02115.
Marshall ThomasProgram in Cellular and Molecular Medicine, Boston Children's Hospital, Boston, MA 02115.
Judy LiebermanProgram in Cellular and Molecular Medicine, Boston Children's Hospital, Boston, MA 02115.
Gerald M McInerneyDepartment of Microbiology, Tumor and Cell Biology, Karolinska Institutet, Stockholm SE-171 77, Sweden.
Pavel IvanovDivision of Rheumatology, Immunology and Allergy, Harvard Medical School and Brigham and Women's Hospital, Boston, MA 02115 The Broad Institute of Harvard and MIT, Cambridge, MA 02142.
Paul AndersonDivision of Rheumatology, Immunology and Allergy, Harvard Medical School and Brigham and Women's Hospital, Boston, MA 02115.

Funding

Stress granules and cell signalingR01GM111700 · NIGMS · BRIGHAM AND WOMEN'S HOSPITAL · PI ANDERSON, PAUL J. · 2014 to 2017
$1.3M
Angiogenin-Induced RNA Cleavage in CancerR01CA168872 · NCI · BRIGHAM AND WOMEN'S HOSPITAL · PI ANDERSON, PAUL J. · 2013 to 2015
$1.1M
G-quadruplex Structures as Targets and Tools in ALSR21NS094918 · NINDS · BRIGHAM AND WOMEN'S HOSPITAL · PI IVANOV, PAVEL · 2015 to 2016
$488k
NCI NIH HHS CA168872NCI NIH HHS R01 CA168872NIAID NIH HHS AI0655858NIGMS NIH HHS R01 GM111700NINDS NIH HHS NS094918NINDS NIH HHS R21 NS094918
6 · The paper itself

Abstract

Mammalian stress granules (SGs) contain stalled translation preinitiation complexes that are assembled into discrete granules by specific RNA-binding proteins such as G3BP. We now show that cells lacking both G3BP1 and G3BP2 cannot form SGs in response to eukaryotic initiation factor 2α phosphorylation or eIF4A inhibition, but are still SG-competent when challenged with severe heat or osmotic stress. Rescue experiments using G3BP1 mutants show that phosphomimetic G3BP1-S149E fails to rescue SG formation, whereas G3BP1-F33W, a mutant unable to bind G3BP partner proteins Caprin1 or USP10, rescues SG formation. Caprin1/USP10 binding to G3BP is mutually exclusive: Caprin binding promotes, but USP10 binding inhibits, SG formation. G3BP interacts with 40S ribosomal subunits through its RGG motif, which is also required for G3BP-mediated SG formation. We propose that G3BP mediates the condensation of SGs by shifting between two different states that are controlled by the phosphorylation of S149 and by binding to Caprin1 or USP10.

Indexed as

Adaptor Proteins, Signal TransducingAmino Acid SequenceAnimalsBase SequenceCarrier ProteinsCell Cycle ProteinsCell Line, TumorChlorocebus aethiopsCOS CellsCytoplasmic GranulesDNA HelicasesEukaryotic Initiation Factor-2Eukaryotic Initiation Factor-4AHumansMicroscopy, ConfocalMicroscopy, VideoAdaptor Proteins, Signal TransducingCAPRIN1 protein, humanCarrier ProteinsCell Cycle ProteinsDNA HelicasesEukaryotic Initiation Factor-2Eukaryotic Initiation Factor-4AG3BP1 protein, humanG3BP2 protein, humanPoly-ADP-Ribose Binding ProteinsRibosomal ProteinsRNA-Binding ProteinsRNA HelicasesRNA Recognition Motif ProteinsUbiquitin ThiolesteraseUSP10 protein, human

Identifiers

PMID27022092
PMCPMC4810302

What OpenQuestion holds

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LicenceCC BY-NC-SA
Read underepoch 390

Registered trials

None linked

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.