Evidence map›Paper›PMID 25034784›Full record

ArticleCell death and differentiation2014

Inhibition of autophagy, lysosome and VCP function impairs stress granule assembly.

S J Seguin, F F Morelli, J Vinet, D Amore, S De Biasi, A Poletti, D C Rubinsztein, S Carra

Abstract read
In one paragraph

Article in Cell death and differentiation, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 125 papers.

0numbers the graph read from it
0cells of the map it votes in
125citing 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

125 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. TSC2 is a stress granule suppressor.bioRxiv : the preprint server for biology · 2026
    Article
  6. Small heat shock proteins and biomolecular condensates.Cellular and molecular life sciences : CMLS · 2026
    Review
  7. Article
  8. Article
  9. Article
  10. Comparative analysis of wavelength-specific UV stress granule formation.bioRxiv : the preprint server for biology · 2026
    Article
  11. Cytoplasmic circular dsDNA is a key constituent of stress granules.bioRxiv : the preprint server for biology · 2026
    Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review

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

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

8 authors.

S J SeguinDipartimento di Scienze Biomediche, Metaboliche e Neuroscienze, Universita' di Modena e Reggio Emilia, Modena, Italy.
F F MorelliDipartimento di Scienze Biomediche, Metaboliche e Neuroscienze, Universita' di Modena e Reggio Emilia, Modena, Italy.
J VinetDipartimento di Scienze Biomediche, Metaboliche e Neuroscienze, Universita' di Modena e Reggio Emilia, Modena, Italy.
D AmoreDipartimento di Scienze Biomediche, Metaboliche e Neuroscienze, Universita' di Modena e Reggio Emilia, Modena, Italy.
S De BiasiDipartimento Chirurgico, Medico, Odontoiatrico e di Scienze Morfologiche, Universita' di Modena e Reggio Emilia, Modena, Italy.
A PolettiDipartimento di Scienze Farmacologiche e Biomolecolari (DiSFeB), Universita' di Milano, Milan, Italy.
D C RubinszteinDepartment of Medical Genetics, Cambridge Institute for Medical Research, University of Cambridge, Hills Road, Cambridge, UK.
S CarraDipartimento di Scienze Biomediche, Metaboliche e Neuroscienze, Universita' di Modena e Reggio Emilia, Modena, Italy.

Funding

Wellcome Trust 095317Wellcome Trust 100140
6 · The paper itself

Abstract

Stress granules (SGs) are mRNA-protein aggregates induced during stress, which accumulate in many neurodegenerative diseases. Previously, the autophagy-lysosome pathway and valosin-containing protein (VCP), key players of the protein quality control (PQC), were shown to regulate SG degradation. This is consistent with the idea that PQC may survey and/or assist SG dynamics. However, despite these observations, it is currently unknown whether the PQC actively participates in SG assembly. Here, we describe that inhibition of autophagy, lysosomes and VCP causes defective SG formation after induction. Silencing the VCP co-factors UFD1L and PLAA, which degrade defective ribosomal products (DRIPs) and 60S ribosomes, also impaired SG assembly. Intriguingly, DRIPs and 60S, which are released from disassembling polysomes and are normally excluded from SGs, were significantly retained within SGs in cells with impaired autophagy, lysosome or VCP function. Our results suggest that deregulated autophagy, lysosomal or VCP activities, which occur in several neurodegenerative (VCP-associated) diseases, may alter SG morphology and composition.

Indexed as

AutophagyAdenosine TriphosphatasesCell Cycle ProteinsCytoplasmic GranulesGene Knockdown TechniquesHeLa CellsHumansLysosomesRibosomal ProteinsValosin Containing ProteinAdenosine TriphosphatasesCell Cycle ProteinsRibosomal ProteinsRPL19 protein, humanValosin Containing ProteinVCP protein, human

Identifiers

PMID25034784
PMCPMC4227144

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.