Evidence map›Paper›PMID 31604945›Full record

ArticleNature communications2019

Structural basis for substrate specificity and regulation of nucleotide sugar transporters in the lipid bilayer.

Joanne L Parker, Robin A Corey, Phillip J Stansfeld, Simon Newstead

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.5field-weighted citation impact, top 17% 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

22 citing papers in PubMed, 35 citations in OpenAlex.

  1. Review
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  4. Review
  5. International journal of molecular sciences · 2025
    Review
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  15. Review
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  17. Aberrant Protein Glycosylation in Brain Cancers, with Emphasis on Glioblastoma.Advances in experimental medicine and biology · 2022
    Article
  18. Novel Insights into Selected Disease-Causing Mutations within theInternational journal of molecular sciences · 2020
    Article
  19. Biosynthesis of GlcNAc-richThe Journal of biological chemistry · 2020
    Article
  20. 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 2 institutions in 1 country.

Joanne L ParkerDepartment of Biochemistry, University of Oxford, Oxford, OX1 3QU, UK. joanne.parker@bioch.ox.ac.uk.ORCID http://orcid.org/0000-0003-2964-2720
Robin A CoreyDepartment of Biochemistry, University of Oxford, Oxford, OX1 3QU, UK.
Phillip J StansfeldSchool of Life Sciences & Department of Chemistry, The University of Warwick, Coventry, CV4 7AL, UK. phillip.stansfeld@warwick.ac.uk.ORCID http://orcid.org/0000-0001-8800-7669
Simon NewsteadDepartment of Biochemistry, University of Oxford, Oxford, OX1 3QU, UK. simon.newstead@bioch.ox.ac.uk.ORCID http://orcid.org/0000-0001-7432-2270
University of Oxford · GBUniversity of Warwick · GB

Funding

Biotechnology and Biological Sciences Research Council BB/P01948X/1Biotechnology and Biological Sciences Research Council BB/R002517/1Biotechnology and Biological Sciences Research Council BB/S003339/1Medical Research Council MR/S009213/1Medical Research Council MR/S021043/1Wellcome Trust 102890/Z/13/Z
6 · The paper itself

Abstract

Nucleotide sugars are the activated form of monosaccharides used by glycosyltransferases during glycosylation. In eukaryotes the SLC35 family of solute carriers are responsible for their selective uptake into the Endoplasmic Reticulum or Golgi apparatus. The structure of the yeast GDP-mannose transporter, Vrg4, revealed a requirement for short chain lipids and a marked difference in transport rate between the nucleotide sugar and nucleoside monophosphate, suggesting a complex network of regulatory elements control transport into these organelles. Here we report the crystal structure of the GMP bound complex of Vrg4, revealing the molecular basis for GMP recognition and transport. Molecular dynamics, combined with biochemical analysis, reveal a lipid mediated dimer interface and mechanism for coordinating structural rearrangements during transport. Together these results provide further insight into how SLC35 family transporters function within the secretory pathway and sheds light onto the role that membrane lipids play in regulating transport across the membrane.

Indexed as

Binding SitesGuanosine MonophosphateLipid BilayersMembrane Transport ProteinsModels, ChemicalProtein DomainsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSubstrate SpecificityGuanosine MonophosphateLipid BilayersMembrane Transport ProteinsSaccharomyces cerevisiae ProteinsVRG4 protein, S cerevisiae

Identifiers

PMID31604945
PMCPMC6789118
OpenAlexW2979920490

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.