Evidence map›Paper›PMID 33011305›Full record

ArticleMolecular metabolism2020

β-catenin regulates muscle glucose transport via actin remodelling and M-cadherin binding.

Stewart W C Masson, Brie Sorrenson, Peter R Shepherd, Troy L Merry

Open access · goldAbstract read
In one paragraph

Article in Molecular metabolism, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

19 citing papers in PubMed, 45 citations in OpenAlex.

  1. Article
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  4. The insulin signalling network.Nature metabolism · 2025
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  17. UVR Promotes Keratinocyte Phagocytosis and Skin Pigmentation Through TRPA1 Channels.Clinical, cosmetic and investigational dermatology · 2022
    Article
  18. Article
  19. Metabolic Contributions of Wnt Signaling: More Than Controlling Flight.Frontiers in cell and developmental biology · 2021
    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 1 institution in 1 country.

Stewart W C MassonDiscipline of Nutrition, Faculty of Medical and Health Sciences, The University of Auckland, Auckland, New Zealand; Maurice Wilkins Centre for Molecular Biodiscovery, The University of Auckland, Auckland, New Zealand.
Brie SorrensonDepartment of Molecular Medicine and Pathology, Faculty of Medical and Health Sciences, The University of Auckland, Auckland, New Zealand.
Peter R ShepherdMaurice Wilkins Centre for Molecular Biodiscovery, The University of Auckland, Auckland, New Zealand; Department of Molecular Medicine and Pathology, Faculty of Medical and Health Sciences, The University of Auckland, Auckland, New Zealand.
Troy L MerryDiscipline of Nutrition, Faculty of Medical and Health Sciences, The University of Auckland, Auckland, New Zealand; Maurice Wilkins Centre for Molecular Biodiscovery, The University of Auckland, Auckland, New Zealand. Electronic address: t.merry@auckland.ac.nz.
University of Auckland · NZ

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

objectiveSkeletal muscle glucose disposal following a meal is mediated through insulin-stimulated movement of the GLUT4-containing vesicles to the cell surface. The highly conserved scaffold-protein β-catenin is an emerging regulator of vesicle trafficking in other tissues. Here, we investigated the involvement of β-catenin in skeletal muscle insulin-stimulated glucose transport.

methodsGlucose homeostasis and transport was investigated in inducible muscle specific β-catenin knockout (BCAT-mKO) mice. The effect of β-catenin deletion and mutation of β-catenin serine 552 on signal transduction, glucose uptake and protein-protein interactions were determined in L6-G4-myc cells, and β-catenin insulin-responsive binding partners were identified via immunoprecipitation coupled to label-free proteomics.

resultsSkeletal muscle specific deletion of β-catenin impaired whole-body insulin sensitivity and insulin-stimulated glucose uptake into muscle independent of canonical Wnt signalling. In response to insulin, β-catenin was phosphorylated at serine 552 in an Akt-dependent manner, and in L6-G4-myc cells, mutation of β-catenin

conclusionsOur data suggest that β-catenin is a novel mediator of glucose transport in skeletal muscle and may contribute to insulin-induced actin-cytoskeleton remodelling to support GLUT4 translocation.

Indexed as

ActinsAnimalsbeta CateninBiological TransportCadherinsGlucoseGlucose Transporter Type 4Glucose Transport Proteins, FacilitativeInsulinInsulin ResistanceMaleMiceMice, Inbred C57BLMice, KnockoutMuscle, SkeletalProtein BindingActinsbeta CateninCadherinsGlucoseGlucose Transporter Type 4Glucose Transport Proteins, FacilitativeInsulinSlc2a4 protein, mouseActin-remodellingBeta-cateninGlucose transportGLUT4 traffickingM-cadherin

Identifiers

PMID33011305
PMCPMC7568189
OpenAlexW3089507301

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.