Evidence map›Paper›PMID 24389104›Full record

ArticleMolecular cell2014

Ubiquitin ligase trapping identifies an SCF(Saf1) pathway targeting unprocessed vacuolar/lysosomal proteins.

Kevin G Mark, Marco Simonetta, Alessio Maiolica, Charles A Seller, David P Toczyski

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

36 citing papers in PubMed, 55 citations in OpenAlex.

  1. Review
  2. Article
  3. Cul5bioRxiv : the preprint server for biology · 2025
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  7. Insights in Post-Translational Modifications: Ubiquitin and SUMO.International journal of molecular sciences · 2022
    Review
  8. Review
  9. More Than Just Cleaning: Ubiquitin-Mediated Proteolysis in Fungal Pathogenesis.Frontiers in cellular and infection microbiology · 2021
    Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Resolving the Complexity of Ubiquitin Networks.Frontiers in molecular biosciences · 2020
    Review
  15. Article
  16. Review
  17. Review
  18. Article
  19. Article
  20. 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 2 institutions in 2 countries.

Kevin G MarkDepartment of Biochemistry and Biophysics, Helen Diller Family Comprehensive Cancer Center, San Francisco, CA 94158, USA.
Marco SimonettaDepartment of Biochemistry and Biophysics, Helen Diller Family Comprehensive Cancer Center, San Francisco, CA 94158, USA.
Alessio MaiolicaDepartment of Biology, Institute of Molecular Systems Biology, ETH Zürich, Zürich CH-8093, Switzerland.
Charles A SellerDepartment of Biochemistry and Biophysics, Helen Diller Family Comprehensive Cancer Center, San Francisco, CA 94158, USA.
David P ToczyskiDepartment of Biochemistry and Biophysics, Helen Diller Family Comprehensive Cancer Center, San Francisco, CA 94158, USA. Electronic address: toczyski@cc.ucsf.edu.
UCSF Helen Diller Family Comprehensive Cancer Center · USETH Zurich · CH

Funding

GENETICS OF EUCARYOTIC AND PROCARYOTIC ORGANISMST32GM007810 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI ASHRAFI, KAVEH, NARLIKAR, GEETA J · 1985 to 2020
$15.1M
Structure and function of the APCR01GM070539 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI TOCZYSKI, DAVID PAUL · 2004 to 2015
$3.9M
NIGMS NIH HHS GM 70539NIGMS NIH HHS R01 GM070539NIGMS NIH HHS T32 GM007810
6 · The paper itself

Abstract

We have developed a technique, called Ubiquitin Ligase Substrate Trapping, for the isolation of ubiquitinated substrates in complex with their ubiquitin ligase (E3). By fusing a ubiquitin-associated (UBA) domain to an E3 ligase, we were able to selectively purify the polyubiquitinated forms of E3 substrates. Using ligase traps of eight different F box proteins (SCF specificity factors) coupled with mass spectrometry, we identified known, as well as previously unreported, substrates. Polyubiquitinated forms of candidate substrates associated with their cognate F box partner, but not other ligase traps. Interestingly, the four most abundant candidate substrates identified for the F box protein Saf1 were all vacuolar/lysosomal proteins. Analysis of one of these substrates, Prb1, showed that Saf1 selectively promotes ubiquitination of the unprocessed form of the zymogen. This suggests that Saf1 is part of a pathway that targets protein precursors for proteasomal degradation.

Indexed as

F-Box ProteinsLysosomesMass SpectrometryProtein Structure, TertiarySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitinated ProteinsUbiquitinationUbiquitin-Protein LigasesVacuolesF-Box ProteinsSaccharomyces cerevisiae ProteinsSaf1 protein, S cerevisiaeUbiquitinated ProteinsUbiquitin-Protein Ligases

Identifiers

PMID24389104
PMCPMC4032118
OpenAlexW2148466105

What OpenQuestion holds

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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.