Evidence map›Paper›PMID 33619693›Full record

ArticleCell stress & chaperones2021

Protein products of nonstop mRNA disrupt nucleolar homeostasis.

Zoe H Davis, Laura Mediani, Francesco Antoniani, Jonathan Vinet, Shuangxi Li, Simon Alberti, Bingwei Lu, Alex S Holehouse, Serena Carra, Onn Brandman

Abstract read
In one paragraph

Article in Cell stress & chaperones, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing 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

8 citing papers in PubMed.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Review
  7. Quality control of cytoplasmic proteins inside the nucleus.Computational and structural biotechnology journal · 2022
    Review
  8. Review
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

10 authors.

Zoe H DavisDepartment of Biochemistry, Stanford University, Stanford, CA, 94305, USA.
Laura MedianiCentre for Neuroscience and Nanotechnology, Department of Biomedical, Metabolic and Neural Sciences, University of Modena and Reggio, Emilia, Modena, Italy.
Francesco AntonianiCentre for Neuroscience and Nanotechnology, Department of Biomedical, Metabolic and Neural Sciences, University of Modena and Reggio, Emilia, Modena, Italy.
Jonathan VinetCentre for Neuroscience and Nanotechnology, Department of Biomedical, Metabolic and Neural Sciences, University of Modena and Reggio, Emilia, Modena, Italy.
Shuangxi LiDepartment of Pathology, Stanford University, Stanford, CA, 94305, USA.
Simon AlbertiBiotechnology Center (BIOTEC), Center for Molecular and Cellular Bioengineering (CMCB), Technische Universitat Dresden, Tatzberg 47/49, 01307, Dresden, Germany.
Bingwei LuDepartment of Pathology, Stanford University, Stanford, CA, 94305, USA.
Alex S HolehouseDepartment of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, MO, 63110, USA.
Serena CarraCentre for Neuroscience and Nanotechnology, Department of Biomedical, Metabolic and Neural Sciences, University of Modena and Reggio, Emilia, Modena, Italy. serena.carra@unimore.it.
Onn BrandmanDepartment of Biochemistry, Stanford University, Stanford, CA, 94305, USA. onn@stanford.edu.ORCID http://orcid.org/0000-0002-2084-154X

Funding

Molecular Genetic Analysis of TORC1 and TORC2 Signaling in Neuronal MaintenanceR01NS084412 · NINDS · STANFORD UNIVERSITY · PI Bingwei Lu · 2014 to 2026
$4.9M
Genetic Control of Neural Stem Cell HomeostasisR01NS083417 · NINDS · STANFORD UNIVERSITY · PI LU, BINGWEI · 2013 to 2022
$3.5M
Request for Support to Purchase Automated MicroscopeR01GM115968 · NIGMS · STANFORD UNIVERSITY · PI BRANDMAN, ONN · 2015 to 2023
$2.9M
Mitochondrial inner membrane architecture in skeletal muscle pathophysiologyR01AR074875 · NIAMS · STANFORD UNIVERSITY · PI LU, BINGWEI · 2019 to 2023
$2.0M
NIAMS NIH HHS R01 AR074875NIGMS NIH HHS R01 GM115968NIH HHS R01AR0748750NINDS NIH HHS R01 NS083417NINDS NIH HHS R01 NS084412
6 · The paper itself

Abstract

Stalled mRNA translation results in the production of incompletely synthesized proteins that are targeted for degradation by ribosome-associated quality control (RQC). Here we investigated the fate of defective proteins translated from stall-inducing, nonstop mRNA that escape ubiquitylation by the RQC protein LTN1. We found that nonstop protein products accumulated in nucleoli and this localization was driven by polylysine tracts produced by translation of the poly(A) tails of nonstop mRNA. Nucleolar sequestration increased the solubility of invading proteins but disrupted nucleoli, altering their dynamics, morphology, and resistance to stress in cell culture and intact flies. Our work elucidates how stalled translation may affect distal cellular processes and may inform studies on the pathology of diseases caused by failures in RQC and characterized by nucleolar stress.

Indexed as

HomeostasisHumansProtein BiosynthesisRibosomesRNA, MessengerSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitinationUbiquitin-Protein LigasesRNA, MessengerSaccharomyces cerevisiae ProteinsUbiquitin-Protein LigasesLTN1Nonstop mRNANucleolusPhase separationProtein quality controlRibosome-associated quality control (RQC)

Identifiers

PMID33619693
PMCPMC8065075

What OpenQuestion holds

Textmetadata
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.