Evidence map›Paper›PMID 28298493›Full record

ArticleMolecular biology of the cell2017

Deubiquitinating enzymes Ubp2 and Ubp15 regulate endocytosis by limiting ubiquitination and degradation of ARTs.

Hsuan-Chung Ho, Jason A MacGurn, Scott D Emr

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

24 citing papers in PubMed, 39 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. α-Arrestins and Their Functions: From Yeast to Human Health.International journal of molecular sciences · 2022
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Adaptors as the regulators of HECT ubiquitin ligases.Cell death and differentiation · 2021
    Review
  11. Review
  12. Induction and Repression of Hydrolase Genes inFrontiers in microbiology · 2021
    Review
  13. Article
  14. Article
  15. Review
  16. Review
  17. Article
  18. Article
  19. Article
  20. Review
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

3 authors at 2 institutions in 1 country.

Hsuan-Chung HoWeill Institute for Cell and Molecular Biology, Cornell University, Ithaca, NY 14853.
Jason A MacGurnDepartment of Cell and Developmental Biology, Vanderbilt University, Nashville, TN 37240.
Scott D EmrWeill Institute for Cell and Molecular Biology, Cornell University, Ithaca, NY 14853 sde26@cornell.edu.
Cornell University · USVanderbilt University · US

Funding

Substrate Targeting Mechanisms of Nedd4 Family Ubiquitin LigasesR00GM101077 · NIGMS · VANDERBILT UNIVERSITY · PI MACGURN, JASON A · 2014 to 2016
$747k
NIGMS NIH HHS R00 GM101077
6 · The paper itself

Abstract

Endocytic down-regulation of cell-surface proteins is a fundamental cellular process for cell survival and adaptation to environmental stimuli. Ubiquitination of cargo proteins serves as the sorting signal for downstream trafficking and relies on the arrestin-related trafficking adaptor (ART)-Rsp5 ubiquitin ligase adaptor network in yeast. Hence proper regulation of the abundance and activity of these ligase-adaptor complexes is critical for main-tenance of optimal plasma membrane protein composition. Here we report that the stability of ARTs is regulated by the deubiquitinating enzymes (DUBs) Ubp2 and Ubp15. By counteracting the E3 ubiquitin ligase Rsp5, Ubp2 and Ubp15 prevent hyperubiquitination and proteasomal degradation of ARTs. Specifically, we show that loss of both Ubp2 and Ubp15 results in a defect in Hxt6 endocytosis associated with Art4 instability. Our results uncover a novel function for DUBs in the endocytic pathway by which Ubp2 and Ubp15 positively regulate the ART-Rsp5 network.

Indexed as

ArrestinsCell MembraneDeubiquitinating EnzymesEndocytosisEndopeptidasesEndosomal Sorting Complexes Required for TransportProtein BindingProtein TransportSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitinUbiquitinationUbiquitin-Protein Ligase ComplexesUbiquitin-Protein LigasesArrestinsDeubiquitinating EnzymesEndopeptidasesEndosomal Sorting Complexes Required for TransportSaccharomyces cerevisiae ProteinsUbiquitinubiquitin-Nalpha-protein hydrolaseUbiquitin-Protein Ligase ComplexesUbiquitin-Protein LigasesUbp15 protein, S cerevisiae

Identifiers

PMID28298493
PMCPMC5415021
OpenAlexW2605793213

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.