Evidence map›Paper›PMID 23493405›Full record

ArticlePlant physiology2013

Specialized roles of the conserved subunit OST3/6 of the oligosaccharyltransferase complex in innate immunity and tolerance to abiotic stresses.

Akhlaq Farid, Frederikke Gro Malinovsky, Christiane Veit, Jennifer Schoberer, Cyril Zipfel, Richard Strasser

Open access · hybridAbstract read
In one paragraph

Article in Plant physiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
3.4field-weighted citation impact, top 7% 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

31 citing papers in PubMed, 64 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Analysis of Protein Glycosylation in the ER.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  5. Review
  6. An oligosaccharyltransferase fromFrontiers in plant science · 2023
    Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Analysis of Protein Glycosylation in the ER.Methods in molecular biology (Clifton, N.J.) · 2018
    Article
  19. Plant protein glycosylation.Glycobiology · 2016
    Review
  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

6 authors at 2 institutions in 2 countries.

Akhlaq FaridDepartment of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, 1190 Vienna, Austria.
Frederikke Gro Malinovsky
Christiane Veit
Jennifer Schoberer
Cyril Zipfel
Richard Strasser
BOKU University · ATSainsbury Laboratory · GB

Funding

Austrian Science Fund FWF P 23906Biotechnology and Biological Sciences Research Council BB/E024874/1Biotechnology and Biological Sciences Research Council BB/G024944/1
6 · The paper itself

Abstract

Asparagine-linked glycosylation of proteins is an essential cotranslational and posttranslational protein modification in plants. The central step in this process is the transfer of a preassembled oligosaccharide to nascent proteins in the endoplasmic reticulum by the oligosaccharyltransferase (OST) complex. Despite the importance of the catalyzed reaction, the composition and the function of individual OST subunits are still ill defined in plants. Here, we report the function of the highly conserved OST subunit OST3/6. We have identified a mutant in the OST3/6 gene that causes overall underglycosylation of proteins and affects the biogenesis of the receptor kinase EF-TU RECEPTOR involved in innate immunity and the endo-β-1,4-glucanase KORRIGAN1 required for cellulose biosynthesis. Notably, the ost3/6 mutation does not affect mutant variants of the receptor kinase BRASSINOSTEROID-INSENSITIVE1. OST3/6 deficiency results in activation of the unfolded protein response and causes hypersensitivity to salt/osmotic stress and to the glycosylation inhibitor tunicamycin. Consistent with its role in protein glycosylation, OST3/6 resides in the endoplasmic reticulum and interacts with other subunits of the OST complex. Together, our findings reveal the importance of Arabidopsis (Arabidopsis thaliana) OST3/6 for the efficient glycosylation of specific glycoproteins involved in different physiological processes and shed light on the composition and function of the plant OST complex.

Indexed as

Plant ImmunityStress, PhysiologicalAmino Acid SequenceArabidopsisArabidopsis ProteinsCellulaseCelluloseEndoplasmic ReticulumGlycoproteinsGlycosylationHexosyltransferasesMannitolMembrane ProteinsMolecular Sequence DataMutationProtein Interaction MappingArabidopsis ProteinsAt1g61790 protein, ArabidopsisBRI1 protein, ArabidopsisCellulaseCellulosedolichyl-diphosphooligosaccharide - protein glycotransferaseEFR protein, ArabidopsisGlycoproteinsHexosyltransferasesKOR1 protein, ArabidopsisMannitolMembrane ProteinsProtein KinasesReceptors, Pattern RecognitionRecombinant Fusion ProteinsSodium ChlorideTunicamycin

Identifiers

PMID23493405
PMCPMC3641206
OpenAlexW2010683890

What OpenQuestion holds

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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.