Evidence map›Paper›PMID 28746877›Full record

ArticleCell reports2017

Phospho-Rasputin Stabilization by Sec16 Is Required for Stress Granule Formation upon Amino Acid Starvation.

Angelica Aguilera-Gomez, Margarita Zacharogianni, Marinke M van Oorschot, Heide Genau, Rianne Grond, Tineke Veenendaal, Kristina S Sinsimer, Elizabeth R Gavis, Christian Behrends, Catherine Rabouille

Erratum issuedAbstract read
In one paragraph

Article in Cell reports, 2017. 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 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing 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

23 citing papers in PubMed.

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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

10 authors.

Angelica Aguilera-GomezHubrecht Institute-KNAW & University Medical Center (UMC) Utrecht, Uppsalalaan 8, 3584 CT Utrecht, the Netherlands.
Margarita ZacharogianniHubrecht Institute-KNAW & University Medical Center (UMC) Utrecht, Uppsalalaan 8, 3584 CT Utrecht, the Netherlands.
Marinke M van OorschotHubrecht Institute-KNAW & University Medical Center (UMC) Utrecht, Uppsalalaan 8, 3584 CT Utrecht, the Netherlands.
Heide GenauInstitute of Biochemistry II, Medical School Goethe University, 60323 Frankfurt am Main, Germany.
Rianne GrondHubrecht Institute-KNAW & University Medical Center (UMC) Utrecht, Uppsalalaan 8, 3584 CT Utrecht, the Netherlands.
Tineke VeenendaalDepartment of Cell Biology, UMC Utrecht, 3584 CT Utrecht, the Netherlands.
Kristina S SinsimerDepartment of Molecular Biology, Princeton University, Washington Road, Princeton, NJ 08544, USA.
Elizabeth R GavisDepartment of Molecular Biology, Princeton University, Washington Road, Princeton, NJ 08544, USA.
Christian BehrendsInstitute of Biochemistry II, Medical School Goethe University, 60323 Frankfurt am Main, Germany.
Catherine RabouilleHubrecht Institute-KNAW & University Medical Center (UMC) Utrecht, Uppsalalaan 8, 3584 CT Utrecht, the Netherlands; Department of Cell Biology, UMC Utrecht, 3584 CT Utrecht, the Netherlands; Department of Cell Biology, UMC Groningen, 9713 GZ Groningen, the Netherlands. Electronic address: c.rabouille@hubrecht.eu.

Funding

Translational Regulation of Patterning in DrosphilaR01GM061107 · NIGMS · PRINCETON UNIVERSITY · PI GAVIS, ELIZABETH R · 2001 to 2017
$5.2M
NIGMS NIH HHS R01 GM061107
6 · The paper itself

Abstract

Most cellular stresses induce protein translation inhibition and stress granule formation. Here, using Drosophila S2 cells, we investigate the role of G3BP/Rasputin in this process. In contrast to arsenite treatment, where dephosphorylated Ser142 Rasputin is recruited to stress granules, we find that, upon amino acid starvation, only the phosphorylated Ser142 form is recruited. Furthermore, we identify Sec16, a component of the endoplasmic reticulum exit site, as a Rasputin interactor and stabilizer. Sec16 depletion results in Rasputin degradation and inhibition of stress granule formation. However, in the absence of Sec16, pharmacological stabilization of Rasputin is not enough to rescue the assembly of stress granules. This is because Sec16 specifically interacts with phosphorylated Ser142 Rasputin, the form required for stress granule formation upon amino acid starvation. Taken together, these results demonstrate that stress granule formation is fine-tuned by specific signaling cues that are unique to each stress. These results also expand the role of Sec16 as a stress response protein.

Indexed as

Amino AcidsAnimalsCarrier ProteinsCytoplasmic GranulesDrosophilaDrosophila ProteinsImmunoprecipitationPhosphorylationProtein Processing, Post-TranslationalSignal TransductionVesicular Transport ProteinsAmino AcidsCarrier ProteinsDrosophila Proteinsrin protein, DrosophilaSec16 protein, DrosophilaVesicular Transport Proteinsamino acid starvationarseniteDrosophila S2 cellselF2 alphaphosphorylationprotein stabilizationprotein translationprotein transport in the secretory pathwayRasputinSec16stress granulesstress response

Identifiers

PMID28746877
PMCPMC6064189

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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.