Evidence map›Paper›PMID 11847109›Full record

ArticleThe EMBO journal2002

Role of the ubiquitin-selective CDC48(UFD1/NPL4 )chaperone (segregase) in ERAD of OLE1 and other substrates.

Sigurd Braun, Kai Matuschewski, Michael Rape, Sven Thoms, Stefan Jentsch

Abstract read
In one paragraph

Article in The EMBO journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 134 papers.

0numbers the graph read from it
0cells of the map it votes in
134citing papers in PubMed
–field-weighted citation impact
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

134 citing papers in PubMed.

  1. Review
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  4. VCP controls KCC2 degradation through FAF1 recruitment and accelerates emergence from anesthesia.Proceedings of the National Academy of Sciences of the United States of America · 2025
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  8. USP7 and VCPCell reports · 2021
    Article
  9. Review
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  12. Review
  13. The Cryo-EM Effect: Structural Biology of Neurodegenerative Disease Proteostasis Factors.Journal of neuropathology and experimental neurology · 2021
    Review
  14. Article
  15. Review
  16. Article
  17. Review
  18. Review
  19. Protein quality control in the secretory pathway.The Journal of cell biology · 2019
    Review
  20. Article

74 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

5 authors.

Sigurd BraunDepartment of Molecular Cell Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18a, D-82152 Martinsried, Germany.
Kai Matuschewski
Michael Rape
Sven Thoms
Stefan Jentsch

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The OLE pathway of yeast regulates the abundance of the ER-bound enzyme Delta-9 fatty acid desaturase OLE1, thereby controlling unsaturated fatty acid pools and membrane fluidity. Previously, we showed that this pathway is exquisitely regulated by the ubiquitin/proteasome system. Activation of the pathway involves proteasomal processing of a membrane-bound transcription factor and the subsequent mobilization of the cleaved, ubiquitylated transcription factor from its partner molecule by CDC48(UFD1/NPL4), a ubiquitin-selective chaperone-like enzyme. Here we report that the OLE1 protein itself is naturally short-lived and is degraded by ubiquitin/proteasome-dependent ER-associated degradation (ERAD). We found that CDC48(UFD1/NPL4) plays a second role in the OLE pathway by mediating ERAD of OLE1. Intriguingly, other ERAD substrates also require CDC48(UFD1/NPL4) for degradation, indicating that this enzyme is a novel, constitutive component of the ERAD machinery. We propose that CDC48(UFD1/NPL4) functions as a segregase that liberates ubiquitylated proteins from non-modified partners.

Indexed as

Nuclear Pore Complex ProteinsAdenosine TriphosphatasesAmino Acid SequenceCell Cycle ProteinsMolecular Sequence DataNuclear ProteinsNucleocytoplasmic Transport ProteinsSaccharomyces cerevisiae ProteinsSequence Homology, Amino AcidUbiquitinValosin Containing ProteinVesicular Transport ProteinsAdenosine TriphosphatasesCDC48 protein, S cerevisiaeCell Cycle ProteinsNPL4 protein, S cerevisiaeNuclear Pore Complex ProteinsNuclear ProteinsNucleocytoplasmic Transport ProteinsSaccharomyces cerevisiae ProteinsUbiquitinUFD1 protein, S cerevisiaeValosin Containing ProteinVesicular Transport Proteins

Identifiers

PMID11847109
PMCPMC125867

What OpenQuestion holds

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Registered trials

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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.