Evidence map›Paper›PMID 35735144›Full record

ArticleBioscience reports2022

EFR3 and phosphatidylinositol 4-kinase IIIα regulate insulin-stimulated glucose transport and GLUT4 dispersal in 3T3-L1 adipocytes.

Anna M Koester, Angéline Geiser, Kamilla M E Laidlaw, Silke Morris, Marie F A Cutiongco, Laura Stirrat, Nikolaj Gadegaard, Eckhard Boles, Hannah L Black, Nia J Bryant and 1 more

Open access · goldAbstract read
In one paragraph

Article in Bioscience reports, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.0field-weighted citation impact, top 27% 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

11 citing papers in PubMed, 11 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Advanced optical microscopy methods forBiophysical reviews · 2025
    Review
  5. Review
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  7. Review
  8. Article
  9. Benchmarking Thiolate-Driven Photoswitching of Cyanine Dyes.The journal of physical chemistry. B · 2023
    Article
  10. Article
  11. GLUT4 On the move.The Biochemical journal · 2022
    Article
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

11 authors at 5 institutions in 3 countries.

Anna M Koester *Institute for Molecular, Cellular and Systems Biology, University of Glasgow, U.K.
Angéline Geiser *Strathclyde Institute of Pharmacy and Biomedical Sciences, University of Strathclyde, Glasgow, U.K.
Kamilla M E Laidlaw *Institute for Molecular, Cellular and Systems Biology, University of Glasgow, U.K.
Silke MorrisInstitute for Molecular, Cellular and Systems Biology, University of Glasgow, U.K.
Marie F A CutiongcoJames Watt School of Engineering, University of Glasgow, U.K.
Laura StirratStrathclyde Institute of Pharmacy and Biomedical Sciences, University of Strathclyde, Glasgow, U.K.
Nikolaj GadegaardJames Watt School of Engineering, University of Glasgow, U.K.
Eckhard BolesInstitute for Molecular Biosciences, Goethe-University 60438 Frankfurt, Germany.
Hannah L BlackDepartment of Biology and York Biomedical Research Institute, University of York, York, U.K.
Nia J BryantDepartment of Biology and York Biomedical Research Institute, University of York, York, U.K.
Gwyn W GouldInstitute for Molecular, Cellular and Systems Biology, University of Glasgow, U.K.ORCID 0000-0001-6571-2875
University of Strathclyde · GBInstitut de Biologie Moléculaire et Cellulaire · FRUniversity of Glasgow · GBUniversity of York · GBGoethe University Frankfurt · DE

Funding

British Heart Foundation PG/18/47/33822
6 · The paper itself

Abstract

Insulin stimulates glucose transport in muscle and adipocytes. This is achieved by regulated delivery of intracellular glucose transporter (GLUT4)-containing vesicles to the plasma membrane where they dock and fuse, resulting in increased cell surface GLUT4 levels. Recent work identified a potential further regulatory step, in which insulin increases the dispersal of GLUT4 in the plasma membrane away from the sites of vesicle fusion. EFR3 is a scaffold protein that facilitates localization of phosphatidylinositol 4-kinase type IIIα to the cell surface. Here we show that knockdown of EFR3 or phosphatidylinositol 4-kinase type IIIα impairs insulin-stimulated glucose transport in adipocytes. Using direct stochastic reconstruction microscopy, we also show that EFR3 knockdown impairs insulin stimulated GLUT4 dispersal in the plasma membrane. We propose that EFR3 plays a previously unidentified role in controlling insulin-stimulated glucose transport by facilitating dispersal of GLUT4 within the plasma membrane.

Indexed as

1-Phosphatidylinositol 4-KinaseInsulin3T3-L1 CellsAdipocytesAnimalsBiological TransportCell MembraneGlucoseGlucose Transporter Type 4Glucose Transport Proteins, FacilitativeMice1-Phosphatidylinositol 4-KinaseGlucoseGlucose Transporter Type 4Glucose Transport Proteins, FacilitativeInsulinadipocytesglucose transportGLUT4insulin

Identifiers

PMID35735144
PMCPMC9272592
OpenAlexW4283329188

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.