Evidence map›Paper›PMID 30207830›Full record

ArticleMolecular biology of the cell2018

A balance of deubiquitinating enzymes controls cell cycle entry.

Claudine E Mapa, Heather E Arsenault, Michelle M Conti, Kristin E Poti, Jennifer A Benanti

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2018. 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
1.4field-weighted citation impact, top 18% 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, 19 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Ubiquitin-Specific Protease 29 Regulates Cdc25A-Mediated Tumorigenesis.International journal of molecular sciences · 2021
    Article
  7. Article
  8. Review
  9. Review
  10. Article
  11. Dissecting the mechanisms of cell division.The Journal of biological chemistry · 2019
    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

5 authors at 1 institution in 1 country.

Claudine E MapaDepartment of Molecular, Cell and Cancer Biology, University of Massachusetts Medical School, Worcester, MA 01605.
Heather E ArsenaultDepartment of Molecular, Cell and Cancer Biology, University of Massachusetts Medical School, Worcester, MA 01605.
Michelle M ContiDepartment of Molecular, Cell and Cancer Biology, University of Massachusetts Medical School, Worcester, MA 01605.
Kristin E PotiDepartment of Molecular, Cell and Cancer Biology, University of Massachusetts Medical School, Worcester, MA 01605.
Jennifer A BenantiDepartment of Molecular, Cell and Cancer Biology, University of Massachusetts Medical School, Worcester, MA 01605.
University of Massachusetts Chan Medical School · US

Funding

Training: Molecular & Cellular Bases of Infectious DiseasesT32AI007417 · NIAID · JOHNS HOPKINS UNIVERSITY · PI Arturo Casadevall · 1994 to 2026
$11.9M
Translational Cancer Biology Training ProgramT32CA130807 · NCI · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI MERCURIO, ARTHUR M · 2008 to 2018
$2.7M
Cell cycle regulation of chromosome structureR01GM115708 · NIGMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI BENANTI, JENNIFER A · 2016 to 2020
$1.8M
NCI NIH HHS T32 CA130807NIAID NIH HHS T32 AI007417NIGMS NIH HHS R01 GM115708
6 · The paper itself

Abstract

Protein degradation during the cell cycle is controlled by the opposing activities of ubiquitin ligases and deubiquitinating enzymes (DUBs). Although the functions of ubiquitin ligases in the cell cycle have been studied extensively, the roles of DUBs in this process are less well understood. Here, we used an overexpression screen to examine the specificities of each of the 21 DUBs in budding yeast for 37 cell cycle-regulated proteins. We find that DUBs up-regulate specific subsets of proteins, with five DUBs regulating the greatest number of targets. Overexpression of Ubp10 had the largest effect, stabilizing 15 targets and delaying cells in mitosis. Importantly, UBP10 deletion decreased the stability of the cell cycle regulator Dbf4, delayed the G1/S transition, and slowed proliferation. Remarkably, deletion of UBP10 together with deletion of four additional DUBs restored proliferation to near-wild-type levels. Among this group, deletion of the proteasome-associated DUB Ubp6 alone reversed the G1/S delay and restored the stability of Ubp10 targets in ubp10Δ cells. Similarly, deletion of UBP14, another DUB that promotes proteasomal activity, rescued the proliferation defect in ubp10Δ cells. Our results suggest that DUBs function through a complex genetic network in which their activities are coordinated to facilitate accurate cell cycle progression.

Indexed as

Cell CycleCell Cycle ProteinsCell DivisionDeubiquitinating EnzymesGene Regulatory NetworksNuclear ProteinsProteasome Endopeptidase ComplexProteolysisSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSaccharomycetalesUbiquitinUbiquitinationUbiquitin ThiolesteraseCell Cycle ProteinsDeubiquitinating EnzymesNuclear ProteinsProteasome Endopeptidase ComplexSaccharomyces cerevisiae ProteinsUbiquitinUbiquitin ThiolesteraseUBP10 protein, S cerevisiae

Identifiers

PMID30207830
PMCPMC6249862
OpenAlexW2889660697

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.