Evidence map›Paper›PMID 23793018›Full record

ArticleMolecular & cellular proteomics : MCP2013

Perturbations to the ubiquitin conjugate proteome in yeast δubx mutants identify Ubx2 as a regulator of membrane lipid composition.

Natalie Kolawa, Michael J Sweredoski, Robert L J Graham, Robert Oania, Sonja Hess, Raymond J Deshaies

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.5field-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

15 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Science translational medicine · 2021
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Lipid droplet dynamics in budding yeast.Cellular and molecular life sciences : CMLS · 2015
    Review
  13. Article
  14. Article
  15. 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

6 authors at 1 institution in 1 country.

Natalie KolawaDivision of Biology.
Michael J Sweredoski
Robert L J Graham
Robert Oania
Sonja Hess
Raymond J Deshaies
California Institute of Technology · US

Funding

Howard Hughes Medical Institute
6 · The paper itself

Abstract

Yeast Cdc48 (p97/VCP in human cells) is a hexameric AAA ATPase that is thought to use ATP hydrolysis to power the segregation of ubiquitin-conjugated proteins from tightly bound partners. Current models posit that Cdc48 is linked to its substrates through adaptor proteins, including a family of seven proteins (13 in human) that contain a Cdc48-binding UBX domain. However, few substrates for specific UBX proteins are known, and hence the generality of this hypothesis remains untested. Here, we use mass spectrometry to identify ubiquitin conjugates that accumulate in cdc48 and ubx mutants. Different ubx mutants exhibit unique patterns of conjugate accumulation that point to functional specialization of individual Ubx proteins. To validate our findings, we examined in detail the endoplasmic reticulum-bound transcription factor Spt23, which we identified as a putative Ubx2 substrate. Mutant ubx2Δ cells are deficient in both cleaving the ubiquitinated 120 kDa precursor of Spt23 to form active p90 and in localizing p90 to the nucleus, resulting in reduced expression of the target gene OLE1, which encodes fatty acid desaturase. Our findings provide a resource for future investigations on Cdc48, illustrate the utility of proteomics to identify ligands for specific ubiquitin receptor pathways, and uncover Ubx2 as a key player in the regulation of membrane lipid biosynthesis.

Indexed as

Adenosine TriphosphatasesCarrier ProteinsCell Cycle ProteinsMembrane LipidsMembrane ProteinsMutationProteomeSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTranscription FactorsUbiquitinValosin Containing ProteinAdenosine TriphosphatasesCarrier ProteinsCDC48 protein, S cerevisiaeCell Cycle ProteinsMembrane LipidsMembrane ProteinsMGA2 protein, S cerevisiaeProteomeSaccharomyces cerevisiae ProteinsSPT23 protein, S cerevisiaeTranscription FactorsUbiquitinUBX2 protein, S cerevisiaeValosin Containing ProteinVCP protein, human

Identifiers

PMID23793018
PMCPMC3790291
OpenAlexW2140622962

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.