Evidence map›Paper›PMID 29514933›Full record

ArticleMolecular biology of the cell2018

The yeast arrestin-related protein Bul1 is a novel actor of glucose-induced endocytosis.

Junie Hovsepian, Véronique Albanèse, Michel Becuwe, Vasyl Ivashov, David Teis, Sébastien Léon

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
2.1field-weighted citation impact, top 14% 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

14 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
  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. Adaptors as the regulators of HECT ubiquitin ligases.Cell death and differentiation · 2021
    Review
  9. Article
  10. Review
  11. Review
  12. AMPK-Mediated Regulation of Alpha-Arrestins and Protein Trafficking.International journal of molecular sciences · 2019
    Review
  13. Article
  14. 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

6 authors at 2 institutions in 2 countries.

Junie HovsepianInstitut Jacques Monod, UMR 7592 Centre National de la Recherche Scientifique/Université Paris-Diderot, Sorbonne Paris Cité, 75205 Paris, France.
Véronique AlbanèseInstitut Jacques Monod, UMR 7592 Centre National de la Recherche Scientifique/Université Paris-Diderot, Sorbonne Paris Cité, 75205 Paris, France.
Michel BecuweInstitut Jacques Monod, UMR 7592 Centre National de la Recherche Scientifique/Université Paris-Diderot, Sorbonne Paris Cité, 75205 Paris, France.
Vasyl IvashovDivision of Cell Biology, Biocenter, Medical University of Innsbruck, 6020 Innsbruck, Austria.
David TeisDivision of Cell Biology, Biocenter, Medical University of Innsbruck, 6020 Innsbruck, Austria.
Sébastien LéonInstitut Jacques Monod, UMR 7592 Centre National de la Recherche Scientifique/Université Paris-Diderot, Sorbonne Paris Cité, 75205 Paris, France.
Université Paris Cité · FRInnsbruck Medical University · AT

Funding

Austrian Science Fund FWF Y 444
6 · The paper itself

Abstract

Yeast cells have a remarkable ability to adapt to nutritional changes in their environment. During adaptation, nutrient-signaling pathways drive the selective endocytosis of nutrient transporters present at the cell surface. A current challenge is to understand the mechanistic basis of this regulation. Transporter endocytosis is triggered by their ubiquitylation, which involves the ubiquitin ligase Rsp5 and its adaptors of the arrestin-related family (ART). This step is highly regulated by nutrient availability. For instance, the monocarboxylate transporter Jen1 is ubiquitylated, endocytosed, and degraded upon exposure to glucose. The ART protein Rod1 is required for this overall process; yet Rod1 rather controls Jen1 trafficking later in the endocytic pathway and is almost dispensable for Jen1 internalization. Thus, how glucose triggers Jen1 internalization remains unclear. We report that another ART named Bul1, but not its paralogue Bul2, contributes to Jen1 internalization. Bul1 responds to glucose availability, and preferentially acts at the plasma membrane for Jen1 internalization. Thus, multiple ARTs can act sequentially along the endocytic pathway to control transporter homeostasis. Moreover, Bul1 is in charge of Jen1 endocytosis after cycloheximide treatment, suggesting that the functional redundancy of ARTs may be explained by their ability to interact with multiple cargoes in various conditions.

Indexed as

Adaptor Proteins, Signal TransducingArrestinsCell MembraneEndocytosisEndosomal Sorting Complexes Required for TransportGlucoseMembrane ProteinsMembrane Transport ProteinsMonocarboxylic Acid TransportersProtein TransportSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSignal TransductionSymportersUbiquitinUbiquitinationAdaptor Proteins, Signal TransducingArrestinsBUL1 protein, S cerevisiaeBUL2 protein, S cerevisiaeEndosomal Sorting Complexes Required for TransportGlucoseJEN1 protein, S cerevisiaeMembrane ProteinsMembrane Transport ProteinsMonocarboxylic Acid TransportersSaccharomyces cerevisiae ProteinsSymportersUbiquitinUbiquitin-Protein Ligase ComplexesUbiquitin-Protein Ligases

Identifiers

PMID29514933
PMCPMC5921569
OpenAlexW2791332428

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.