Evidence map›Paper›PMID 29467282›Full record

ArticleEMBO reports2018

Proteomic profiling of VCP substrates links VCP to K6-linked ubiquitylation and c-Myc function.

Jan B Heidelberger, Andrea Voigt, Marina E Borisova, Giuseppe Petrosino, Stefanie Ruf, Sebastian A Wagner, Petra Beli

Open access · bronzeAbstract read
In one paragraph

Article in EMBO reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 83 papers.

0numbers the graph read from it
0cells of the map it votes in
83citing papers in PubMed
3.7field-weighted citation impact, top 6% 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

83 citing papers in PubMed, 145 citations in OpenAlex.

  1. Article
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  7. SMARCD1 and Its Functional Relevance in SWI/SNF and Cancer.International journal of molecular sciences · 2026
    Review
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  15. The functional landscape of the human ubiquitinome.bioRxiv : the preprint server for biology · 2025
    Article
  16. Review
  17. Review
  18. Article
  19. Article
  20. Article

23 more citing papers are in PubMed but not listed here.

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

7 authors at 2 institutions in 1 country.

Jan B HeidelbergerInstitute of Molecular Biology (IMB), Mainz, Germany.
Andrea VoigtInstitute of Molecular Biology (IMB), Mainz, Germany.
Marina E BorisovaInstitute of Molecular Biology (IMB), Mainz, Germany.
Giuseppe PetrosinoInstitute of Molecular Biology (IMB), Mainz, Germany.
Stefanie RufInstitute of Molecular Biology (IMB), Mainz, Germany.
Sebastian A WagnerDepartment of Medicine, Hematology/Oncology, Goethe University School of Medicine, Frankfurt, Germany swagner@med.uni-frankfurt.de p.beli@imb-mainz.de.ORCID 0000-0002-8629-6310
Petra BeliInstitute of Molecular Biology (IMB), Mainz, Germany swagner@med.uni-frankfurt.de p.beli@imb-mainz.de.ORCID 0000-0001-9507-9820
Institute of Molecular Biology · DEGoethe University Frankfurt · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Valosin-containing protein (VCP) is an evolutionarily conserved ubiquitin-dependent ATPase that mediates the degradation of proteins through the ubiquitin-proteasome pathway. Despite the central role of VCP in the regulation of protein homeostasis, identity and nature of its cellular substrates remain poorly defined. Here, we combined chemical inhibition of VCP and quantitative ubiquitin remnant profiling to assess the effect of VCP inhibition on the ubiquitin-modified proteome and to probe the substrate spectrum of VCP in human cells. We demonstrate that inhibition of VCP perturbs cellular ubiquitylation and increases ubiquitylation of a different subset of proteins compared to proteasome inhibition. VCP inhibition globally upregulates K6-linked ubiquitylation that is dependent on the HECT-type ubiquitin E3 ligase HUWE1. We report ~450 putative VCP substrates, many of which function in nuclear processes, including gene expression, DNA repair and cell cycle. Moreover, we identify that VCP regulates the level and activity of the transcription factor c-Myc.

Indexed as

Cell LineCell NucleusHumansModels, BiologicalProteasome Endopeptidase ComplexProtein BindingProtein Interaction MappingProtein Interaction MapsProtein TransportProteolysisProteomeProteomicsProto-Oncogene Proteins c-mycUbiquitinationValosin Containing ProteinProteasome Endopeptidase ComplexProteomeProto-Oncogene Proteins c-mycValosin Containing ProteinVCP protein, humanc‐MycHUWE1K6‐linked ubiquitylationubiquitin remnant profilingVCP

Identifiers

PMID29467282
PMCPMC5891417
OpenAlexW2788428532

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.