Evidence map›Paper›PMID 26503781›Full record

ArticleMolecular and cellular biology2016

The Catalytic Activity of the Ubp3 Deubiquitinating Protease Is Required for Efficient Stress Granule Assembly in Saccharomyces cerevisiae.

Regina Nostramo, Sapna N Varia, Bo Zhang, Megan M Emerson, Paul K Herman

Open access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed, 1 pooled it
2.0field-weighted citation impact, top 14% 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

32 citing papers in PubMed, 1 synthesis or guideline pooled it, 52 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Research progress of DUB enzyme in breast cancer.Clinical and experimental medicine · 2025
    Review
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  13. Review
  14. Article
  15. Article
  16. Review
  17. Article
  18. Cuminal InhibitsMicroorganisms · 2020
    Article
  19. Article
  20. 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

5 authors at 1 institution in 1 country.

Regina NostramoDepartment of Molecular Genetics, The Ohio State University, Columbus, Ohio, USA.
Sapna N VariaDepartment of Molecular Genetics, The Ohio State University, Columbus, Ohio, USA.
Bo ZhangDepartment of Molecular Genetics, The Ohio State University, Columbus, Ohio, USA.
Megan M EmersonDepartment of Molecular Genetics, The Ohio State University, Columbus, Ohio, USA.
Paul K HermanDepartment of Molecular Genetics, The Ohio State University, Columbus, Ohio, USA herman.81@osu.edu.
The Ohio State University · US

Funding

The regulation of autophagy pathways in eukaryotic cellsR01GM065227 · NIGMS · OHIO STATE UNIVERSITY · PI HERMAN, PAUL K · 2002 to 2014
$3.6M
The regulation and function of cytoplasmic foci in quiescent cellsR01GM101191 · NIGMS · OHIO STATE UNIVERSITY · PI HERMAN, PAUL K · 2013 to 2016
$1.2M
NIGMS NIH HHS GM065227NIGMS NIH HHS GM101191NIGMS NIH HHS R01 GM065227NIGMS NIH HHS R01 GM101191
6 · The paper itself

Abstract

The interior of the eukaryotic cell is a highly compartmentalized space containing both membrane-bound organelles and the recently identified nonmembranous ribonucleoprotein (RNP) granules. This study examines in Saccharomyces cerevisiae the assembly of one conserved type of the latter compartment, known as the stress granule. Stress granules form in response to particular environmental cues and have been linked to a variety of human diseases, including amyotrophic lateral sclerosis. To further our understanding of these structures, a candidate genetic screen was employed to identify regulators of stress granule assembly in quiescent cells. These studies identified a ubiquitin-specific protease, Ubp3, as having an essential role in the assembly of these RNP granules. This function was not shared by other members of the Ubp protease family and required Ubp3 catalytic activity as well as its interaction with the cofactor Bre5. Interestingly, the loss of stress granules was correlated with a decrease in the long-term survival of stationary-phase cells. This phenotype is similar to that observed in mutants defective for the formation of a related RNP complex, the Processing body. Altogether, these observations raise the interesting possibility of a general role for these types of cytoplasmic RNP granules in the survival of G0-like resting cells.

Indexed as

BiocatalysisCytoplasmic GranulesEndopeptidasesOrganellesProtein Processing, Post-TranslationalRibonucleoproteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsStress, PhysiologicalEndopeptidasesRibonucleoproteinsSaccharomyces cerevisiae ProteinsUBP3 protein, S cerevisiae

Identifiers

PMID26503781
PMCPMC4702605
OpenAlexW2209057621

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.