Evidence map›Paper›PMID 29355480›Full record

ArticleeLife2018

Sorting of a multi-subunit ubiquitin ligase complex in the endolysosome system.

Xi Yang, Felichi Mae Arines, Weichao Zhang, Ming Li

Abstract read
In one paragraph

Article in eLife, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing 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

22 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. The Dsc complex and its role in Golgi quality control.Biochemical Society transactions · 2024
    Review
  7. Article
  8. Article
  9. Ubiquitin-mediated degradation at the Golgi apparatus.Frontiers in molecular biosciences · 2023
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Exogenous HAging and disease · 2020
    Article
  18. Article
  19. Protein quality control in the secretory pathway.The Journal of cell biology · 2019
    Review
  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

4 authors.

Xi YangDepartment of Molecular, Cellular and Developmental Biology, University of Michigan, Ann Arbor, United States.ORCID http://orcid.org/0000-0003-2741-2294
Felichi Mae ArinesDepartment of Molecular, Cellular and Developmental Biology, University of Michigan, Ann Arbor, United States.ORCID http://orcid.org/0000-0002-5770-3116
Weichao ZhangDepartment of Molecular, Cellular and Developmental Biology, University of Michigan, Ann Arbor, United States.ORCID http://orcid.org/0000-0002-0835-890X
Ming LiDepartment of Molecular, Cellular and Developmental Biology, University of Michigan, Ann Arbor, United States.ORCID http://orcid.org/0000-0002-1247-2377

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The yeast Dsc E3 ligase complex has long been recognized as a Golgi-specific protein ubquitination system. It shares a striking sequence similarity to the Hrd1 complex that plays critical roles in the ER-associated degradation pathway. Using biochemical purification and mass spectrometry, we identified two novel Dsc subunits, which we named as Gld1 and Vld1. Surprisingly, Gld1 and Vld1 do not coexist in the same complex. Instead, they compete with each other to form two functionally independent Dsc subcomplexes. The Vld1 subcomplex takes the AP3 pathway to reach the vacuole membrane, whereas the Gld1 subcomplex travels through the VPS pathway and is cycled between Golgi and endosomes by the retromer. Thus, instead of being Golgi-specific, the Dsc complex can regulate protein levels at three distinct organelles, namely Golgi, endosome, and vacuole. Our study provides a novel model of achieving multi-tasking for transmembrane ubiquitin ligases with interchangeable trafficking adaptors.

Indexed as

EndosomesGolgi ApparatusProtein SubunitsProtein TransportSaccharomyces cerevisiaeUbiquitin-Protein LigasesVacuolesProtein SubunitsUbiquitin-Protein Ligasesbiochemistrycell biologyDsc E3 ligase complexendosomegolgilysosomeprotein ubiquitinationS. cerevisiae

Identifiers

PMID29355480
PMCPMC5811209

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.