Evidence map›Paper›PMID 23424197›Full record

ArticleJournal of cell science2013

Endosomal sorting of GLUT4 and Gap1 is conserved between yeast and insulin-sensitive cells.

Annette M Shewan, Rebecca K McCann, Christopher A Lamb, Laura Stirrat, Dimitrios Kioumourtzoglou, Iain S Adamson, Suzie Verma, David E James, Nia J Bryant

Abstract read
In one paragraph

Article in Journal of cell science, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.3field-weighted citation impact, top 39% 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

7 citing papers in PubMed, 11 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. A proteolytic pathway that controls glucose uptake in fat and muscle.Reviews in endocrine & metabolic disorders · 2014
    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

9 authors at 3 institutions in 2 countries.

Annette M ShewanSchool of Chemistry and Molecular Bioscience, University of Queensland, St. Lucia QLD 4072, Australia. a.shewan@uq.edu.au
Rebecca K McCann
Christopher A Lamb
Laura Stirrat
Dimitrios Kioumourtzoglou
Iain S Adamson
Suzie Verma
David E James
Nia J Bryant
University of Glasgow · GBUniversity of Queensland · AUGarvan Institute of Medical Research · AU

Funding

Medical Research Council MR/J000221/1Wellcome Trust 081933/Z/07/Z
6 · The paper itself

Abstract

The insulin-regulated trafficking of the facilitative glucose transporter GLUT4 in human fat and muscle cells and the nitrogen-regulated trafficking of the general amino acid permease Gap1 in the yeast Saccharomyces cerevisiae share several common features: Both Gap1 and GLUT4 are nutrient transporters that are mobilised to the cell surface from an intracellular store in response to an environmental cue; both are polytopic membrane proteins harbouring amino acid targeting motifs in their C-terminal tails that are required for their regulated trafficking; ubiquitylation of both Gap1 and GLUT4 plays an important role in their regulated trafficking, as do the ubiquitin-binding GGA (Golgi-localised, γ-ear-containing, ARF-binding) adaptor proteins. Here, we find that when expressed heterologously in yeast, human GLUT4 is subject to nitrogen-regulated trafficking in an ubiquitin-dependent manner similar to Gap1. In addition, by expressing a GLUT4/Gap1 chimeric protein in adipocytes we show that the carboxy-tail of Gap1 directs intracellular sequestration and insulin-regulated trafficking in adipocytes. These findings demonstrate that the trafficking signals and their cognate molecular regulatory machinery that mediate regulated exocytosis of membrane proteins are conserved across evolution.

Indexed as

3T3-L1 CellsAdipocytesAnimalsEndosomesFluorescent Antibody Technique, IndirectGlucose Transporter Type 4GTPase-Activating ProteinsImmunoblottingMiceProtein TransportSaccharomyces cerevisiaeGlucose Transporter Type 4GTPase-Activating ProteinsEndosomesProtein sortingRegulated traffic

Identifiers

PMID23424197
PMCPMC3647436
OpenAlexW2115232390

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.