Evidence map›Paper›PMID 21707802›Full record

ArticleThe Plant journal : for cell and molecular biology2011

Arabidopsis thaliana alpha1,2-glucosyltransferase (ALG10) is required for efficient N-glycosylation and leaf growth.

Akhlaq Farid, Martin Pabst, Jennifer Schoberer, Friedrich Altmann, Josef Glössl, Richard Strasser

Open access · bronzeAbstract read
In one paragraph

Article in The Plant journal : for cell and molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

35 citing papers in PubMed, 50 citations in OpenAlex.

  1. Review
  2. Analysis of Protein Glycosylation in the ER.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  3. Article
  4. Article
  5. Disentangling leaf-microbiome interactions inFrontiers in plant science · 2022
    Article
  6. Article
  7. Review
  8. Article
  9. Fine mapping and identification of the leaf shape gene BoFL in ornamental kale.TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2020
    Article
  10. Frontiers in plant science · 2020
    Review
  11. Review
  12. Lack of the α1,3-Fucosyltransferase Gene (International journal of molecular sciences · 2018
    Article
  13. The glycan-dependent ERAD machinery degrades topologically diverse misfolded proteins.The Plant journal : for cell and molecular biology · 2018
    Article
  14. Article
  15. Article
  16. Analysis of Protein Glycosylation in the ER.Methods in molecular biology (Clifton, N.J.) · 2018
    Article
  17. Article
  18. 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, BOKU-University of Natural Resources and Life Sciences, Muthgasse 18, A-1190 Vienna, Austria.
Martin Pabst
Jennifer Schoberer
Friedrich Altmann
Josef Glössl
Richard Strasser
BOKU University · ATOxford Brookes University · GB

Funding

Austrian Science Fund FWF P 20817
6 · The paper itself

Abstract

Assembly of the dolichol-linked oligosaccharide precursor (Glc(3) Man(9) GlcNAc(2) ) is highly conserved among eukaryotes. In contrast to yeast and mammals, little is known about the biosynthesis of dolichol-linked oligosaccharides and the transfer to asparagine residues of nascent polypeptides in plants. To understand the biological function of these processes in plants we characterized the Arabidopsis thaliana homolog of yeast ALG10, the α1,2-glucosyltransferase that transfers the terminal glucose residue to the lipid-linked precursor. Expression of an Arabidopsis ALG10-GFP fusion protein in Nicotiana benthamiana leaf epidermal cells revealed a reticular distribution pattern resembling endoplasmic reticulum (ER) localization. Analysis of lipid-linked oligosaccharides showed that Arabidopsis ALG10 can complement the yeast Δalg10 mutant strain. A homozygous Arabidopsis T-DNA insertion mutant (alg10-1) accumulated mainly lipid-linked Glc(2) Man(9) GlcNAc(2) and displayed a severe protein underglycosylation defect. Phenotypic analysis of alg10-1 showed that mutant plants have altered leaf size when grown in soil. Moreover, the inactivation of ALG10 in Arabidopsis resulted in the activation of the unfolded protein response, increased salt sensitivity and suppression of the phenotype of α-glucosidase I-deficient plants. In summary, these data show that Arabidopsis ALG10 is an ER-resident α1,2-glucosyltransferase that is required for lipid-linked oligosaccharide biosynthesis and subsequently for normal leaf development and abiotic stress response.

Indexed as

ArabidopsisArabidopsis ProteinsCarbohydrate SequenceEndoplasmic ReticulumGenetic Complementation TestGlucosyltransferasesGlycosylationGreen Fluorescent ProteinsMolecular Sequence DataMutagenesis, InsertionalNicotianaOligosaccharidesPhenotypePlant LeavesPolyisoprenyl Phosphate SugarsPolysaccharidesALG10 protein, ArabidopsisArabidopsis ProteinsGlc(3)Man(9)(GlcNAc)(2)-diphosphate-dolicholGlucosyltransferasesGreen Fluorescent ProteinsOligosaccharidesPolyisoprenyl Phosphate SugarsPolysaccharides

Identifiers

PMID21707802
PMCPMC3204403
OpenAlexW2159997962

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Registered trials

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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.