Evidence map›Paper›PMID 21187394›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2011

Conserved endoplasmic reticulum-associated degradation system to eliminate mutated receptor-like kinases in Arabidopsis.

Wei Su, Yidan Liu, Yang Xia, Zhi Hong, Jianming Li

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 papers.

0numbers the graph read from it
0cells of the map it votes in
69citing papers in PubMed
11.2field-weighted citation impact, top 2% 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

69 citing papers in PubMed, 119 citations in OpenAlex.

  1. Review
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  8. Molecular Lesions in BRI1 and Its Orthologs in the Plant Kingdom.International journal of molecular sciences · 2024
    Review
  9. Article
  10. Article
  11. Review
  12. Mechanisms of Endoplasmic Reticulum Protein Homeostasis in Plants.International journal of molecular sciences · 2023
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Article

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

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

5 authors at 1 institution in 2 countries.

Wei SuDepartment of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI 48109-1048, USA.
Yidan Liu
Yang Xia
Zhi Hong
Jianming Li
University of Michigan–Ann Arbor · US

Funding

MOLECULAR GENETIC STUDIES OF PLANT STEROID SIGNALINGR01GM060519 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI LI, JIANMING · 2000 to 2008
$2.3M
NIGMS NIH HHS GM060519NIGMS NIH HHS R01 GM060519
6 · The paper itself

Abstract

Endoplasmic reticulum (ER)-associated degradation (ERAD) is an integral part of the ER quality-control system that removes toxic misfolded proteins via ubiquitin/proteasome-mediated degradation. Most of our knowledge on ERAD comes from biochemical and genetic studies in yeast and mammalian cells. Although ERAD is known to operate in plant cells, little is known about its molecular components and its biochemical mechanism. A genetic screen for suppressors of the Arabidopsis bri1-9, a weak dwarf mutant caused by ER retention of a structurally defective yet biochemically competent brassinosteroid (BR) receptor BRI1, resulted in identification of the EMS-mutagenized bri1 suppressor 5 (EBS5) gene that encodes an Arabidopsis homolog of the yeast Hrd3/mammalian Sel1L protein known to be involved in ERAD. Loss-of-function ebs5 mutations block the ERAD of bri1-9 and bri1-5, another ER-retained BR receptor. We showed that EBS5 complemented the ERAD defect of the yeast Δhrd3 mutant and interacted with the two mutated BR receptors in plant cells. Using a reverse genetic approach, we discovered that two Arabidopsis homologs of the yeast/mammalian Hrd1, an ER membrane-localized ubiquitin ligase, function redundantly in the ERAD of bri1-9. Together, our results revealed functional roles of two conserved ERAD components in degrading mutated/misfolded receptor-like kinases in Arabidopsis.

Indexed as

MutationArabidopsisArabidopsis ProteinsCloning, MolecularCycloheximideEndoplasmic ReticulumGenetic Complementation TestGlycoproteinsImmunoprecipitationProtein DenaturationProtein FoldingReceptors, SteroidTime FactorsTransgenesUbiquitin-Protein LigasesArabidopsis ProteinsCycloheximideGlycoproteinsReceptors, SteroidUbiquitin-Protein Ligases

Identifiers

PMID21187394
PMCPMC3021050
OpenAlexW2002580292

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.