Evidence map›Paper›PMID 26371323›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2015

EBS7 is a plant-specific component of a highly conserved endoplasmic reticulum-associated degradation system in Arabidopsis.

Yidan Liu, Congcong Zhang, Dinghe Wang, Wei Su, Linchuan Liu, Muyang Wang, Jianming Li

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
2.0field-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

40 citing papers in PubMed, 63 citations in OpenAlex.

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

7 authors at 2 institutions in 2 countries.

Yidan LiuDepartment of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI 48109;
Congcong ZhangShanghai Center for Plant Stress Biology, Shanghai Institutes for Biological Sciences, The Chinese Academy of Sciences, Shanghai 201602, China.
Dinghe WangShanghai Center for Plant Stress Biology, Shanghai Institutes for Biological Sciences, The Chinese Academy of Sciences, Shanghai 201602, China.
Wei SuDepartment of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI 48109;
Linchuan LiuShanghai Center for Plant Stress Biology, Shanghai Institutes for Biological Sciences, The Chinese Academy of Sciences, Shanghai 201602, China.
Muyang WangShanghai Center for Plant Stress Biology, Shanghai Institutes for Biological Sciences, The Chinese Academy of Sciences, Shanghai 201602, China.
Jianming LiDepartment of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI 48109; Shanghai Center for Plant Stress Biology, Shanghai Institutes for Biological Sciences, The Chinese Academy of Sciences, Shanghai 201602, China jian@umich.edu.
Shanghai Institutes for Biological Sciences · CNUniversity of Michigan–Ann Arbor · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Endoplasmic reticulum (ER)-associated degradation (ERAD) is an essential part of an ER-localized protein quality-control system for eliminating terminally misfolded proteins. Recent studies have demonstrated that the ERAD machinery is conserved among yeast, animals, and plants; however, it remains unknown if the plant ERAD system involves plant-specific components. Here we report that the Arabidopsis ethyl methanesulfonate-mutagenized brassinosteroid-insensitive 1 suppressor 7 (EBS7) gene encodes an ER membrane-localized ERAD component that is highly conserved in land plants. Loss-of-function ebs7 mutations prevent ERAD of brassinosteroid insensitive 1-9 (bri1-9) and bri1-5, two ER-retained mutant variants of the cell-surface receptor for brassinosteroids (BRs). As a result, the two mutant receptors accumulate in the ER and consequently leak to the plasma membrane, resulting in the restoration of BR sensitivity and phenotypic suppression of the bri1-9 and bri1-5 mutants. EBS7 accumulates under ER stress, and its mutations lead to hypersensitivity to ER and salt stresses. EBS7 interacts with the ER membrane-anchored ubiquitin ligase Arabidopsis thaliana HMG-CoA reductase degradation 1a (AtHrd1a), one of the central components of the Arabidopsis ERAD machinery, and an ebs7 mutation destabilizes AtHrd1a to reduce polyubiquitination of bri1-9. Taken together, our results uncover a plant-specific component of a plant ERAD pathway and also suggest its likely biochemical function.

Indexed as

ProteolysisAmino Acid SequenceArabidopsisArabidopsis ProteinsBase SequenceCloning, MolecularEndoplasmic ReticulumEscherichia coliEthyl MethanesulfonateImmunoblottingMembrane ProteinsMicroscopy, ConfocalMolecular Sequence DataOligonucleotidesPlants, Genetically ModifiedPlasmidsArabidopsis ProteinsBRI1 protein, ArabidopsisEBS7 protein, ArabidopsisEthyl MethanesulfonateMembrane ProteinsOligonucleotidesProtein Kinasesbrassinosteroid receptor BRI1EMS-mutagenized bri1 suppressorERADubiquitin ligase E3unfolded protein response

Identifiers

PMID26371323
PMCPMC4593087
OpenAlexW2107278263

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.