Evidence map›Paper›PMID 20739461›Full record

ArticleMolecular biology of the cell2010

Alpha-arrestins Aly1 and Aly2 regulate intracellular trafficking in response to nutrient signaling.

Allyson F O'Donnell, Alex Apffel, Richard G Gardner, Martha S Cyert

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 71 papers.

0numbers the graph read from it
0cells of the map it votes in
71citing 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

71 citing papers in PubMed, 101 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  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. Review
  12. Review
  13. Review
  14. A Library ofFrontiers in bioengineering and biotechnology · 2021
    Article
  15. Article
  16. Identifying New Substrates and Functions for an Old Enzyme: Calcineurin.Cold Spring Harbor perspectives in biology · 2020
    Review
  17. Article
  18. Article
  19. Regulation of Amino Acid Transport in Saccharomyces cerevisiae.Microbiology and molecular biology reviews : MMBR · 2019
    Review
  20. Article

11 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

4 authors at 3 institutions in 1 country.

Allyson F O'DonnellDepartment of Biology, Stanford University, Stanford, CA 94305-5020, USA.
Alex Apffel
Richard G Gardner
Martha S Cyert
Stanford University · USAgilent Technologies (United States) · USUniversity of Washington · US

Funding

NIGMS NIH HHS GM-48728
6 · The paper itself

Abstract

Extracellular signals regulate trafficking events to reorganize proteins at the plasma membrane (PM); however, few effectors of this regulation have been identified. β-Arrestins relay signaling cues to the trafficking machinery by controlling agonist-stimulated endocytosis of G-protein-coupled receptors. In contrast, we show that yeast α-arrestins, Aly1 and Aly2, control intracellular sorting of Gap1, the general amino acid permease, in response to nutrients. These studies are the first to demonstrate association of α-arrestins with clathrin and clathrin adaptor proteins (AP) and show that Aly1 and Aly2 interact directly with the γ-subunit of AP-1, Apl4. Aly2-dependent trafficking of Gap1 requires AP-1, which mediates endosome-to-Golgi transport, and the nutrient-regulated kinase, Npr1, which phosphorylates Aly2. During nitrogen starvation, Npr1 phosphorylation of Aly2 may stimulate Gap1 incorporation into AP-1/clathrin-coated vesicles to promote Gap1 trafficking from endosomes to the trans-Golgi network. Ultimately, increased Aly1-/Aly2-mediated recycling of Gap1 from endosomes results in higher Gap1 levels within cells and at the PM by diverting Gap away from trafficking pathways that lead to vacuolar degradation. This work defines a new role for arrestins in membrane trafficking and offers insight into how α-arrestins coordinate signaling events with protein trafficking.

Indexed as

Amino AcidsArrestinsCell MembraneClathrinEndocytosisEndosomesIntracellular SpaceModels, BiologicalMutationNitrogenProtein BindingProtein TransportSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSignal Transductiontrans-Golgi NetworkAmino AcidsArrestinsClathrinNitrogenSaccharomyces cerevisiae Proteins

Identifiers

PMID20739461
PMCPMC2954120
OpenAlexW2154830357

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.