Evidence map›Paper›PMID 29396984›Full record

ArticleThe Plant journal : for cell and molecular biology2018

The glycan-dependent ERAD machinery degrades topologically diverse misfolded proteins.

Yun-Ji Shin, Ulrike Vavra, Christiane Veit, Richard Strasser

Open access · hybridAbstract read
In one paragraph

Article in The Plant journal : for cell and molecular biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.6field-weighted citation impact, top 18% 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

15 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
  2. Analysis of Protein Glycosylation in the ER.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  3. Review
  4. Article
  5. Article
  6. Interference of ArabidopsisFrontiers in plant science · 2022
    Article
  7. Article
  8. Article
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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 1 institution in 1 country.

Yun-Ji ShinDepartment of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, Muthgasse 18, Vienna, A-1190, Austria.
Ulrike VavraDepartment of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, Muthgasse 18, Vienna, A-1190, Austria.
Christiane VeitDepartment of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, Muthgasse 18, Vienna, A-1190, Austria.
Richard StrasserDepartment of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, Muthgasse 18, Vienna, A-1190, Austria.ORCID 0000-0001-8764-6530
BOKU University · AT

Funding

Austrian Science Fund FWF P 28218
6 · The paper itself

Abstract

Many soluble and integral membrane proteins fold in the endoplasmic reticulum (ER) with the help of chaperones and folding factors. Despite these efforts, protein folding is intrinsically error prone and amino acid changes, alterations in post-translational modifications or cellular stress can cause protein misfolding. Folding-defective non-native proteins are cleared from the ER and typically undergo ER-associated degradation (ERAD). Here, we investigated whether different misfolded glycoproteins require the same set of ERAD factors and are directed to HRD1 complex-mediated degradation in plants. We generated a series of glycoprotein ERAD substrates harboring a misfolded domain from Arabidopsis STRUBBELIG or the BRASSINOSTEROID INSENSITVE 1 receptor fused to different membrane anchoring regions. We show that single pass and multispanning ERAD substrates are subjected to glycan-dependent degradation by the HRD1 complex. However, the presence of a powerful ER exit signal in the multispanning ERAD substrates causes competition with ER quality control and targeting of misfolded glycoproteins to the vacuole. Our results demonstrate that the same machinery is used for degradation of topologically different misfolded glycoproteins in the ER of plants.

Indexed as

Endoplasmic Reticulum-Associated DegradationProtein FoldingArabidopsis ProteinsEndoplasmic ReticulumGlycoproteinsGolgi ApparatusMembrane ProteinsArabidopsis ProteinsGlycoproteinsMembrane Proteinsendoplasmic reticulumglycosylationintegral membrane proteinprotein foldingquality control

Identifiers

PMID29396984
PMCPMC5900737
OpenAlexW2792196409

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.