Evidence map›Paper›PMID 29681524›Full record

ArticleCell chemical biology2018

Structural Lipids Enable the Formation of Functional Oligomers of the Eukaryotic Purine Symporter UapA.

Euan Pyle, Antreas C Kalli, Sotiris Amillis, Zoe Hall, Andy M Lau, Aylin C Hanyaloglu, George Diallinas, Bernadette Byrne, Argyris Politis

Abstract read
In one paragraph

Article in Cell chemical biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
–field-weighted citation impact
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

47 citing papers in PubMed.

  1. Article
  2. The Nanodisc System for Investigating Protein-Lipid Interactions.Methods in molecular biology (Clifton, N.J.) · 2026
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  9. Review
  10. Gas-sensing riboceptors.RNA biology · 2024
    Article
  11. Article
  12. Review
  13. Structure of the human respiratory complex II.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors.

Euan PyleDepartment of Life Sciences, Imperial College London, London SW7 2AZ, UK; Department of Chemistry, King's College London, London SE1 1DB, UK.
Antreas C KalliLeeds Institute of Cancer & Pathology and Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds LS2 9JT, UK.
Sotiris AmillisDepartment of Biology, National and Kapodistrian University of Athens, Panepistimioupolis, 15781 Athens, Greece.
Zoe HallDepartment of Biochemistry, University of Cambridge, Cambridge CB2 1GA, UK.
Andy M LauDepartment of Chemistry, King's College London, London SE1 1DB, UK.
Aylin C HanyalogluInstitute of Reproductive and Developmental Biology, Department of Surgery and Cancer, Imperial College London, London W12 0NN, UK.
George DiallinasDepartment of Biology, National and Kapodistrian University of Athens, Panepistimioupolis, 15781 Athens, Greece.
Bernadette ByrneDepartment of Life Sciences, Imperial College London, London SW7 2AZ, UK. Electronic address: b.byrne@imperial.ac.uk.
Argyris PolitisDepartment of Chemistry, King's College London, London SE1 1DB, UK. Electronic address: argyris.politis@kcl.ac.uk.

Funding

Biotechnology and Biological Sciences Research Council BB/K017292/1Wellcome TrustWellcome Trust 109854/Z/15/Z
6 · The paper itself

Abstract

The role of membrane lipids in modulating eukaryotic transporter assembly and function remains unclear. We investigated the effect of membrane lipids in the structure and transport activity of the purine transporter UapA from Aspergillus nidulans. We found that UapA exists mainly as a dimer and that two lipid molecules bind per UapA dimer. We identified three phospholipid classes that co-purified with UapA: phosphatidylcholine, phosphatidylethanolamine (PE), and phosphatidylinositol (PI). UapA delipidation caused dissociation of the dimer into monomers. Subsequent addition of PI or PE rescued the UapA dimer and allowed recovery of bound lipids, suggesting a central role of these lipids in stabilizing the dimer. Molecular dynamics simulations predicted a lipid binding site near the UapA dimer interface. Mutational analyses established that lipid binding at this site is essential for formation of functional UapA dimers. We propose that structural lipids have a central role in the formation of functional, dimeric UapA.

Indexed as

Binding SitesEukaryotaFungal ProteinsMembrane Transport ProteinsMolecular Dynamics SimulationMolecular StructurePhospholipidsFungal ProteinsMembrane Transport ProteinsPhospholipidsUAPA protein, Aspergillus nidulanseukaryotic membrane proteinin vivo mutational analysesion-mobility mass spectrometrylipidomicsliquid chromatography-mass spectrometrymembrane protein oligomerizationmolecular dynamics simulationsnative mass spectrometryprotein-lipid interactionsUapA

Identifiers

PMID29681524
PMCPMC6058078

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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.