Evidence map›Paper›PMID 18408158›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2008

Salt tolerance of Arabidopsis thaliana requires maturation of N-glycosylated proteins in the Golgi apparatus.

Jae Sook Kang, Julia Frank, Chang Ho Kang, Hiroyuki Kajiura, Meenu Vikram, Akihiro Ueda, Sewon Kim, Jeong Dong Bahk, Barbara Triplett, Kazuhito Fujiyama and 3 more

Erratum issuedOpen access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 111 papers.

0numbers the graph read from it
0cells of the map it votes in
111citing papers in PubMed
20.0field-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

111 citing papers in PubMed, 243 citations in OpenAlex.

  1. Salinity tolerance in wheat: rethinking the targets.Journal of experimental botany · 2026
    Review
  2. Review
  3. Article
  4. Article
  5. Review
  6. Trafficking and localization of Golgi-residentFrontiers in plant science · 2025
    Review
  7. Review
  8. Review
  9. Article
  10. Review
  11. Analysis of Protein Glycosylation in the ER.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  12. Article
  13. Article
  14. Article
  15. The RNA landscape ofFrontiers in plant science · 2023
    Article
  16. Article
  17. Review
  18. Review
  19. Interference of ArabidopsisFrontiers in plant science · 2022
    Article
  20. Review

51 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

13 authors at 6 institutions in 4 countries.

Jae Sook KangBrain Korea-21, Division of Applied Life Science and Environmental Biotechnology National Core Research Center, Graduate School of Gyeongsang National University, Jinju 660-701, Korea.
Julia Frank
Chang Ho Kang
Hiroyuki Kajiura
Meenu Vikram
Akihiro Ueda
Sewon Kim
Jeong Dong Bahk
Barbara Triplett
Kazuhito Fujiyama
Sang Yeol Lee
Antje von Schaewen
Hisashi Koiwa
Gyeongsang National University · KRTexas A&M University · USUniversity of Münster · DEOsaka University · JPSouthern Regional Research Center · USUnited States Department of Agriculture · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein N-glycosylation in the endoplasmic reticulum (ER) and in the Golgi apparatus is an essential process in eukaryotic cells. Although the N-glycosylation pathway in the ER has been shown to regulate protein quality control, salt tolerance, and cellulose biosynthesis in plants, no biological roles have been linked functionally to N-glycan modifications that occur in the Golgi apparatus. Herein, we provide evidence that mutants defective in N-glycan maturation, such as complex glycan 1 (cgl1), are more salt-sensitive than wild type. Salt stress caused growth inhibition, aberrant root-tip morphology, and callose accumulation in cgl1, which were also observed in an ER oligosaccharyltransferase mutant, staurosporin and temperature sensitive 3a (stt3a). Unlike stt3a, cgl1 did not cause constitutive activation of the unfolded protein response. Instead, aberrant modification of the plasma membrane glycoprotein KORRIGAN 1/RADIALLY SWOLLEN 2 (KOR1/RSW2) that is necessary for cellulose biosynthesis occurred in cgl1 and stt3a. Genetic analyses identified specific interactions among rsw2, stt3a, and cgl1 mutations, indicating that the function of KOR1/RSW2 protein depends on complex N-glycans. Furthermore, cellulose deficient rsw1-1 and rsw2-1 plants were also salt-sensitive. These results establish that plant protein N-glycosylation functions beyond protein folding in the ER and is necessary for sufficient cell-wall formation under salt stress.

Indexed as

SaltsAdaptation, PhysiologicalArabidopsisArabidopsis ProteinsGlycoproteinsGlycosylationGolgi ApparatusArabidopsis ProteinsGlycoproteinsSalts

Identifiers

PMID18408158
PMCPMC2311335
OpenAlexW2096690181

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.