Evidence map›Paper›PMID 24948786›Full record

ArticleG3 (Bethesda, Md.)2014

Histone H2B ubiquitination promotes the function of the anaphase-promoting complex/cyclosome in Schizosaccharomyces pombe.

Zachary C Elmore, Janel R Beckley, Jun-Song Chen, Kathleen L Gould

Open access · goldAbstract read
In one paragraph

Article in G3 (Bethesda, Md.), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.4field-weighted citation impact, top 36% 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

11 citing papers in PubMed, 16 citations in OpenAlex.

  1. Article
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  5. Article
  6. Fission yeast Opy1 is an endogenous PI(4,5)PJournal of cell science · 2020
    Article
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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

4 authors at 1 institution in 1 country.

Zachary C ElmoreDepartment of Cell and Developmental Biology, Vanderbilt University School of Medicine, Nashville, Tennessee 37232.
Janel R BeckleyDepartment of Cell and Developmental Biology, Vanderbilt University School of Medicine, Nashville, Tennessee 37232.
Jun-Song ChenDepartment of Cell and Developmental Biology, Vanderbilt University School of Medicine, Nashville, Tennessee 37232.
Kathleen L GouldDepartment of Cell and Developmental Biology, Vanderbilt University School of Medicine, Nashville, Tennessee 37232 kathy.gould@vanderbilt.edu.
Vanderbilt University · US

Funding

Integrated Biological Systems Training in OncologyT32CA119925 · NCI · VANDERBILT UNIVERSITY · PI Vivian Gama, William Patrick Tansey · 2008 to 2026
$7.6M
NCI NIH HHS 2T32CA119925-06NCI NIH HHS T32 CA119925
6 · The paper itself

Abstract

Ubiquitination and deubiquitination of proteins are reciprocal events involved in many cellular processes, including the cell cycle. During mitosis, the metaphase to anaphase transition is regulated by the ubiquitin ligase activity of the anaphase-promoting complex/cyclosome (APC/C). Although the E3 ubiquitin ligase function of the APC/C has been well characterized, it is not clear whether deubiquitinating enzymes (DUBs) play a role in reversing APC/C substrate ubiquitination. Here we performed a genetic screen to determine what DUB, if any, antagonizes the function of the APC/C in the fission yeast Schizosaccharomyces pombe. We found that deletion of ubp8, encoding the Spt-Ada-Gcn5-Acetyl transferase (SAGA) complex associated DUB, suppressed temperature-sensitive phenotypes of APC/C mutants cut9-665, lid1-6, cut4-533, and slp1-362. Our analysis revealed that Ubp8 antagonizes APC/C function in a mechanism independent of the spindle assembly checkpoint and proteasome activity. Notably, suppression of APC/C mutants was linked to loss of Ubp8 catalytic activity and required histone H2B ubiquitination. On the basis of these data, we conclude that Ubp8 antagonizes APC/C function indirectly by modulating H2B ubiquitination status.

Indexed as

Anaphase-Promoting Complex-CyclosomeEndopeptidasesHistonesSchizosaccharomycesSchizosaccharomyces pombe ProteinsUbiquitinationAnaphase-Promoting Complex-CyclosomeEndopeptidasesHistonesSchizosaccharomyces pombe ProteinsUBP8 protein, S cerevisiaeanaphase promoting complex/cyclosome (APC/C)deubiquitinating enzymes (DUBs)histone H2BSAGA complexubiquitination

Identifiers

PMID24948786
PMCPMC4132182
OpenAlexW2100406431

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.