Evidence map›Paper›PMID 25266656›Full record

ArticleMolecular and cellular biology2014

Substrate-induced ubiquitylation and endocytosis of yeast amino acid permeases.

Kassem Ghaddar, Ahmad Merhi, Elie Saliba, Eva-Maria Krammer, Martine Prévost, Bruno André

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.

0numbers the graph read from it
0cells of the map it votes in
64citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

64 citing papers in PubMed, 108 citations in OpenAlex.

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  13. α-Arrestins and Their Functions: From Yeast to Human Health.International journal of molecular sciences · 2022
    Review
  14. Development and quantitative analysis of a biosensor based on the Arabidopsis SWEET1 sugar transporter.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  15. Article
  16. Review
  17. Article
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4 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

6 authors at 1 institution in 1 country.

Kassem GhaddarMolecular Physiology of the Cell, Université Libre de Bruxelles, IBMM, Gosselies, Belgium.
Ahmad MerhiMolecular Physiology of the Cell, Université Libre de Bruxelles, IBMM, Gosselies, Belgium.
Elie SalibaMolecular Physiology of the Cell, Université Libre de Bruxelles, IBMM, Gosselies, Belgium.
Eva-Maria KrammerStructure and Function of Biological Membranes, Université Libre de Bruxelles, Campus Plaine, Brussels, Belgium.
Martine PrévostStructure and Function of Biological Membranes, Université Libre de Bruxelles, Campus Plaine, Brussels, Belgium.
Bruno AndréMolecular Physiology of the Cell, Université Libre de Bruxelles, IBMM, Gosselies, Belgium bran@ulb.ac.be.
Université Libre de Bruxelles · BE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Many plasma membrane transporters are downregulated by ubiquitylation, endocytosis, and delivery to the lysosome in response to various stimuli. We report here that two amino acid transporters of Saccharomyces cerevisiae, the general amino acid permease (Gap1) and the arginine-specific permease (Can1), undergo ubiquitin-dependent downregulation in response to their substrates and that this downregulation is not due to intracellular accumulation of the transported amino acids but to transport catalysis itself. Following an approach based on permease structural modeling, mutagenesis, and kinetic parameter analysis, we obtained evidence that substrate-induced endocytosis requires transition of the permease to a conformational state preceding substrate release into the cell. Furthermore, this transient conformation must be stable enough, and thus sufficiently populated, for the permease to undergo efficient downregulation. Additional observations, including the constitutive downregulation of two active Gap1 mutants altered in cytosolic regions, support the model that the substrate-induced conformational transition inducing endocytosis involves remodeling of cytosolic regions of the permeases, thereby promoting their recognition by arrestin-like adaptors of the Rsp5 ubiquitin ligase. Similar mechanisms might control many other plasma membrane transporters according to the external concentrations of their substrates.

Indexed as

Amino AcidsAmino Acid Transport SystemsAmino Acid Transport Systems, BasicBinding SitesBiocatalysisEndocytosisEndosomal Sorting Complexes Required for TransportGene Expression Regulation, FungalLysosomesModels, MolecularMutationProtein ConformationProtein Structure, TertiarySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSignal TransductionAmino AcidsAmino Acid Transport SystemsAmino Acid Transport Systems, BasicCAN1 protein, S cerevisiaeEndosomal Sorting Complexes Required for TransportGAP1 protein, S cerevisiaeRSP5 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitin-Protein Ligase Complexes

Identifiers

PMID25266656
PMCPMC4248734
OpenAlexW2135711463

What OpenQuestion holds

Textmetadata
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.