Evidence map›Paper›PMID 23824189›Full record

ArticleThe Journal of biological chemistry2013

A calcineurin-dependent switch controls the trafficking function of α-arrestin Aly1/Art6.

Allyson F O'Donnell, Laiqiang Huang, Jeremy Thorner, Martha S Cyert

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

44 citing papers in PubMed, 64 citations in OpenAlex.

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

4 authors at 3 institutions in 1 country.

Allyson F O'DonnellDepartment of Biology, Stanford University, Stanford, California 94305-5020, USA. allyod@pitt.edu
Laiqiang Huang
Jeremy Thorner
Martha S Cyert
Stanford University · USUniversity of California, Berkeley · USUniversity of Pittsburgh · US

Funding

Yeast Protein Kinase Signaling Networks: Specificity, Regulation and FunctionR01GM021841 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI THORNER, JEREMY W. · 1985 to 2019
$11.8M
Regulation of Dopamine Transporter by TraffickingR01DA014204 · NIDA · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI ALEXANDER D SORKIN · 2001 to 2026
$8.3M
LTQ XL Linear Quadrupole Ion Trap Mass SpectrometerS10RR025622 · NCRR · UNIVERSITY OF CALIFORNIA BERKELEY · PI KOHLSTAEDT, LORI · 2009 to 2009
$463k
NCRR NIH HHS S10 RR025622NCRR NIH HHS S10 RR025622-01NIDA NIH HHS R01 DA014204NIDA NIH HHS R01 DA014204-11NIGMS NIH HHS R01 GM021841NIGMS NIH HHS R01 GM-21841NIGMS NIH HHS R01 GM-48728
6 · The paper itself

Abstract

Proper regulation of plasma membrane protein endocytosis by external stimuli is required for cell growth and survival. In yeast, excess levels of certain nutrients induce endocytosis of the cognate permeases to prevent toxic accumulation of metabolites. The α-arrestins, a family of trafficking adaptors, stimulate ubiquitin-dependent and clathrin-mediated endocytosis by interacting with both a client permease and the ubiquitin ligase Rsp5. However, the molecular mechanisms that control α-arrestin function are not well understood. Here, we show that α-arrestin Aly1/Art6 is a phosphoprotein that specifically interacts with and is dephosphorylated by the Ca(2+)- and calmodulin-dependent phosphoprotein phosphatase calcineurin/PP2B. Dephosphorylation of Aly1 by calcineurin at a subset of phospho-sites is required for Aly1-mediated trafficking of the aspartic acid and glutamic acid transporter Dip5 to the vacuole, but it does not alter Rsp5 binding, ubiquitinylation, or stability of Aly1. In addition, dephosphorylation of Aly1 by calcineurin does not regulate the ability of Aly1 to promote the intracellular sorting of the general amino acid permease Gap1. These results suggest that phosphorylation of Aly1 inhibits its vacuolar trafficking function and, conversely, that dephosphorylation of Aly1 by calcineurin serves as a regulatory switch to promote Aly1-mediated trafficking to the vacuole.

Indexed as

14-3-3 ProteinsAmino Acid MotifsAmino Acid SequenceArrestinsCalcineurinCatalytic DomainChromatography, LiquidEndocytosisHumansMass SpectrometryModels, BiologicalMolecular Sequence DataMutant ProteinsPhenotypePhosphopeptidesPhosphorylation14-3-3 ProteinsAly1 protein, S cerevisiaeArrestinsCalcineurinMutant ProteinsPhosphopeptidesSaccharomyces cerevisiae ProteinsAly1Aly2ArrestinCalcineurinCalciumDip5EndocytosisGap1Nutrient PermeasesTrafficking

Identifiers

PMID23824189
PMCPMC3745350
OpenAlexW2103544547

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.