Evidence map›Paper›PMID 28382714›Full record

ArticleTraffic (Copenhagen, Denmark)2017

Enzyme reversal to explore the function of yeast E3 ubiquitin-ligases.

Chris MacDonald, Stanley Winistorfer, Robert M Pope, Michael E Wright, Robert C Piper

Open access · bronzeAbstract read
In one paragraph

Article in Traffic (Copenhagen, Denmark), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

18 citing papers in PubMed, 36 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Deciphering the RNA-binding protein network during endosomal mRNA transport.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  6. The Dsc complex and its role in Golgi quality control.Biochemical Society transactions · 2024
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. A detrimental mutation on USP40 unlocks the tumorigenesis in a rare case of lung cancer.International journal of clinical and experimental pathology · 2019
    Article
  18. 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.

Chris MacDonaldMolecular Physiology and Biophysics, University of Iowa, Iowa City, Iowa.
Stanley WinistorferMolecular Physiology and Biophysics, University of Iowa, Iowa City, Iowa.
Robert M PopeProteomics Facility, University of Iowa, Iowa City, Iowa.
Michael E WrightMolecular Physiology and Biophysics, University of Iowa, Iowa City, Iowa.
Robert C PiperMolecular Physiology and Biophysics, University of Iowa, Iowa City, Iowa.
University of Iowa · US

Funding

Viral VectorP30CA086862 · NCI · UNIVERSITY OF IOWA · PI Douglas Robert Spitz · 2000 to 2026
$70.0M
Ubiquitin-Dependent Sorting in Endosomes and the TGNR01GM058202 · NIGMS · UNIVERSITY OF IOWA · PI PIPER, ROBERT C · 1998 to 2025
$8.9M
Quantitative mapping of ubiquitin ligase substratesR01GM094830 · NIGMS · UNIVERSITY OF IOWA · PI PIPER, ROBERT C, WRIGHT, MICHAEL E · 2010 to 2013
$1.2M
NIGMS NIH HHS R01 GM058202NIGMS NIH HHS R01 GM094830
6 · The paper itself

Abstract

The covalent attachment of ubiquitin onto proteins can elicit a variety of downstream consequences. Attachment is mediated by a large array of E3 ubiquitin ligases, each thought be subject to regulatory control and to have a specific repertoire of substrates. Assessing the biological roles of ligases, and in particular, identifying their biologically relevant substrates has been a persistent yet challenging question. In this study, we describe tools that may help achieve both of these goals. We describe a strategy whereby the activity of a ubiquitin ligase has been enzymatically reversed, accomplished by fusing it to a catalytic domain of an exogenous deubiquitinating enzyme. We present a library of 72 "anti-ligases" that appear to work in a dominant-negative fashion to stabilize their cognate substrates against ubiquitin-dependent proteasomal and lysosomal degradation. We then used the ligase-deubiquitinating enzyme (DUb) library to screen for E3 ligases involved in post-Golgi/endosomal trafficking. We identify ligases previously implicated in these pathways (Rsp5 and Tul1), in addition to ligases previously localized to endosomes (Pib1 and Vps8). We also document an optimized workflow for isolating and analyzing the "ubiquitome" of yeast, which can be used with mass spectrometry to identify substrates perturbed by expression of particular ligase-DUb fusions.

Indexed as

Endoplasmic Reticulum-Associated DegradationCell MembraneDeubiquitinating EnzymesEndosomal Sorting Complexes Required for TransportEndosomesGolgi ApparatusLysosomesPlasmidsProtein TransportRecombinant Fusion ProteinsSaccharomyces cerevisiae ProteinsUbiquitinUbiquitinationUbiquitin-Protein LigasesDeubiquitinating EnzymesEndosomal Sorting Complexes Required for TransportRecombinant Fusion ProteinsSaccharomyces cerevisiae ProteinsUbiquitinUbiquitin-Protein LigasesE3 ubiquitin ligaseendosomal traffickingER-associated degradation (ERAD)lysosomemass spectrometryproteasomeubiquitinubiquitinationvacuolar protein sorting

Identifiers

PMID28382714
PMCPMC5503471
OpenAlexW2604317607

What OpenQuestion holds

Textmetadata
LicenceTDM
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.