Evidence map›Paper›PMID 27302065›Full record

ArticleThe Journal of biological chemistry2016

Mammalian Glucose Transporter Activity Is Dependent upon Anionic and Conical Phospholipids.

Richard C Hresko, Thomas E Kraft, Andrew Quigley, Elisabeth P Carpenter, Paul W Hruz

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
4.5field-weighted citation impact, top 5% 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

40 citing papers in PubMed, 67 citations in OpenAlex.

  1. Review
  2. Article
  3. A two-step mechanism for sugar translocation.Nature structural & molecular biology · 2026
    Article
  4. Article
  5. Article
  6. Comparative analysis of STP6 and STP10 unravels molecular selectivity in sugar transport proteins.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  7. Article
  8. Article
  9. Review
  10. Over-Production of the Human SLC7A10 inInternational journal of molecular sciences · 2023
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Review
  19. Article
  20. 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

5 authors at 4 institutions in 2 countries.

Richard C HreskoFrom the Departments of Pediatrics and.
Thomas E KraftFrom the Departments of Pediatrics and thomas_kraft@gmx.net.
Andrew Quigleythe Structural Genomics Consortium, University of Oxford, Oxford OX3 7DQ, United Kingdom.
Elisabeth P Carpenterthe Structural Genomics Consortium, University of Oxford, Oxford OX3 7DQ, United Kingdom.
Paul W HruzFrom the Departments of Pediatrics and Cell Biology and Physiology, Washington University School of Medicine, St. Louis, Missouri 63110 and hruz_p@kids.wustl.edu.
Genomics (United Kingdom) · GBPediatrics and Genetics · USUniversity of Oxford · GBWashington University in St. Louis · US

Funding

Wellcome Trust 106169
6 · The paper itself

Abstract

The regulated movement of glucose across mammalian cell membranes is mediated by facilitative glucose transporters (GLUTs) embedded in lipid bilayers. Despite the known importance of phospholipids in regulating protein structure and activity, the lipid-induced effects on the GLUTs remain poorly understood. We systematically examined the effects of physiologically relevant phospholipids on glucose transport in liposomes containing purified GLUT4 and GLUT3. The anionic phospholipids, phosphatidic acid, phosphatidylserine, phosphatidylglycerol, and phosphatidylinositol, were found to be essential for transporter function by activating it and stabilizing its structure. Conical lipids, phosphatidylethanolamine and diacylglycerol, enhanced transporter activity up to 3-fold in the presence of anionic phospholipids but did not stabilize protein structure. Kinetic analyses revealed that both lipids increase the kcat of transport without changing the Km values. These results allowed us to elucidate the activation of GLUT by plasma membrane phospholipids and to extend the field of membrane protein-lipid interactions to the family of structurally and functionally related human solute carriers.

Indexed as

Glucose Transporter Type 3Glucose Transporter Type 4PhospholipidsBiological Transport, ActiveHEK293 CellsHumansLiposomesGlucose Transporter Type 3Glucose Transporter Type 4LiposomesPhospholipidsSLC2A3 protein, humanSLC2A4 protein, humanglucose transportglucose transporter type 3 (GLUT3)glucose transporter type 4 (GLUT4)glucose transport kineticsliposomemembrane transporter reconstitutionphospholipidphospholipid vesicleprotein-lipid interaction

Identifiers

PMID27302065
PMCPMC5016126
OpenAlexW2434912404

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.