Evidence map›Paper›PMID 22249293›Full record

ArticleThe Journal of cell biology2012

A molecular switch on an arrestin-like protein relays glucose signaling to transporter endocytosis.

Michel Becuwe, Neide Vieira, David Lara, Jéssica Gomes-Rezende, Carina Soares-Cunha, Margarida Casal, Rosine Haguenauer-Tsapis, Olivier Vincent, Sandra Paiva, Sébastien Léon

Abstract read
In one paragraph

Article in The Journal of cell biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 85 papers.

0numbers the graph read from it
0cells of the map it votes in
85citing 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

85 citing papers in PubMed.

  1. Article
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  12. α-Arrestins and Their Functions: From Yeast to Human Health.International journal of molecular sciences · 2022
    Review
  13. Review
  14. Article
  15. Article
  16. Review
  17. Article
  18. Review
  19. Adaptors as the regulators of HECT ubiquitin ligases.Cell death and differentiation · 2021
    Review
  20. Article

25 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

10 authors.

Michel BecuweInstitut Jacques Monod, Centre National de la Recherche Scientifique, UMR 7592, Université Paris Diderot, Sorbonne Paris Cité, F-75205 Paris, France.
Neide Vieira
David Lara
Jéssica Gomes-Rezende
Carina Soares-Cunha
Margarida Casal
Rosine Haguenauer-Tsapis
Olivier Vincent
Sandra Paiva
Sébastien Léon

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Endocytosis regulates the plasma membrane protein landscape in response to environmental cues. In yeast, the endocytosis of transporters depends on their ubiquitylation by the Nedd4-like ubiquitin ligase Rsp5, but how extracellular signals trigger this ubiquitylation is unknown. Various carbon source transporters are known to be ubiquitylated and endocytosed when glucose-starved cells are exposed to glucose. We show that this required the conserved arrestin-related protein Rod1/Art4, which was activated in response to glucose addition. Indeed, Rod1 was a direct target of the glucose signaling pathway composed of the AMPK homologue Snf1 and the PP1 phosphatase Glc7/Reg1. Glucose promoted Rod1 dephosphorylation and its subsequent release from a phospho-dependent interaction with 14-3-3 proteins. Consequently, this allowed Rod1 ubiquitylation by Rsp5, which was a prerequisite for transporter endocytosis. This paper therefore demonstrates that the arrestin-related protein Rod1 relays glucose signaling to transporter endocytosis and provides the first molecular insights into the nutrient-induced activation of an arrestin-related protein through a switch in post-translational modifications.

Indexed as

EndocytosisSignal TransductionArrestinEndosomal Sorting Complexes Required for TransportGlucoseGreen Fluorescent ProteinsMembrane ProteinsMembrane Transport ProteinsMonocarboxylic Acid TransportersProtein Processing, Post-TranslationalProtein Serine-Threonine KinasesSaccharomyces cerevisiae ProteinsSymportersUbiquitinationUbiquitin-Protein Ligase ComplexesArrestinEndosomal Sorting Complexes Required for TransportGlucosegreen fluorescent protein, Aequorea victoriaGreen Fluorescent ProteinsJEN1 protein, S cerevisiaeMembrane ProteinsMembrane Transport ProteinsMonocarboxylic Acid TransportersProtein Serine-Threonine KinasesROD1 protein, S cerevisiaeRSP5 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSNF1-related protein kinasesSymportersUbiquitin-Protein Ligase Complexes

Identifiers

PMID22249293
PMCPMC3265958

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Registered trials

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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.