Evidence map›Paper›PMID 23695979›Full record

ArticleThe Plant cell2013

Abnormal glycosphingolipid mannosylation triggers salicylic acid-mediated responses in Arabidopsis.

Jenny C Mortimer, Xiaolan Yu, Sandra Albrecht, Francesca Sicilia, Mariela Huichalaf, Diego Ampuero, Louise V Michaelson, Alex M Murphy, Toshiro Matsunaga, Samantha Kurz and 7 more

Open access · hybridAbstract read
In one paragraph

Article in The Plant cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
15.7field-weighted citation impact, top 1% 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

54 citing papers in PubMed, 93 citations in OpenAlex.

  1. Article
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  3. Genetic Editing ofGenes · 2025
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  8. Review
  9. Article
  10. Article
  11. Diversity in sphingolipid metabolism across land plants.Journal of experimental botany · 2022
    Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Review
  17. Article
  18. Article
  19. ThePlant direct · 2021
    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

17 authors at 6 institutions in 4 countries.

Jenny C MortimerDepartment of Biochemistry, University of Cambridge, Cambridge CB2 1QW, United Kingdom.
Xiaolan Yu
Sandra Albrecht
Francesca Sicilia
Mariela Huichalaf
Diego Ampuero
Louise V Michaelson
Alex M Murphy
Toshiro Matsunaga
Samantha Kurz
Elaine Stephens
Timothy C Baldwin
Tadashi Ishii
Johnathan A Napier
Andreas P M Weber
Michael G Handford
Paul Dupree
University of Cambridge · GBUniversity of Chile · CLForestry and Forest Products Research Institute · JPHeinrich Heine University Düsseldorf · DERothamsted Research · GBUniversity of Wolverhampton · GB

Funding

Biotechnology and Biological Sciences Research Council BB/D010446/1Biotechnology and Biological Sciences Research Council BB/G016240/1Biotechnology and Biological Sciences Research Council BB/H531551/1
6 · The paper itself

Abstract

The Arabidopsis thaliana protein GOLGI-LOCALIZED NUCLEOTIDE SUGAR TRANSPORTER (GONST1) has been previously identified as a GDP-d-mannose transporter. It has been hypothesized that GONST1 provides precursors for the synthesis of cell wall polysaccharides, such as glucomannan. Here, we show that in vitro GONST1 can transport all four plant GDP-sugars. However, gonst1 mutants have no reduction in glucomannan quantity and show no detectable alterations in other cell wall polysaccharides. By contrast, we show that a class of glycosylated sphingolipids (glycosylinositol phosphoceramides [GIPCs]) contains Man and that this mannosylation is affected in gonst1. GONST1 therefore is a Golgi GDP-sugar transporter that specifically supplies GDP-Man to the Golgi lumen for GIPC synthesis. gonst1 plants have a dwarfed phenotype and a constitutive hypersensitive response with elevated salicylic acid levels. This suggests an unexpected role for GIPC sugar decorations in sphingolipid function and plant defense signaling. Additionally, we discuss these data in the context of substrate channeling within the Golgi.

Indexed as

ArabidopsisArabidopsis ProteinsBiological TransportCell WallGlycosphingolipidsGlycosylationGolgi ApparatusGuanosine Diphosphate FucoseGuanosine Diphosphate MannoseGuanosine Diphosphate SugarsImmunoblottingMannoseMembrane Transport ProteinsMicroscopy, FluorescenceMutationSalicylic AcidArabidopsis ProteinsGlycosphingolipidsGONST1 protein, ArabidopsisGuanosine Diphosphate Fucoseguanosine diphosphate glucoseGuanosine Diphosphate MannoseGuanosine Diphosphate SugarsMannoseMembrane Transport ProteinsSalicylic Acid

Identifiers

PMID23695979
PMCPMC3694712
OpenAlexW2167192808

What OpenQuestion holds

Textmetadata
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.