Evidence map›Paper›PMID 29087340›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2017

MPSR1 is a cytoplasmic PQC E3 ligase for eliminating emergent misfolded proteins in

Jong Hum Kim, Seok Keun Cho, Tae Rin Oh, Moon Young Ryu, Seong Wook Yang, Woo Taek Kim

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.5field-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

13 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Genome-Wide Identification and Characterization of Warming-Related Genes inInternational journal of molecular sciences · 2018
    Article
  12. Salicylic acid-independent role of NPR1 is required for protection from proteotoxic stress in the plant endoplasmic reticulum.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  13. 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.

Jong Hum KimDepartment of Systems Biology, College of Life Science and Biotechnology, Yonsei University, Seoul 03722, Republic of Korea.
Seok Keun ChoDepartment of Systems Biology, College of Life Science and Biotechnology, Yonsei University, Seoul 03722, Republic of Korea.
Tae Rin OhDepartment of Systems Biology, College of Life Science and Biotechnology, Yonsei University, Seoul 03722, Republic of Korea.
Moon Young RyuDepartment of Systems Biology, College of Life Science and Biotechnology, Yonsei University, Seoul 03722, Republic of Korea.
Seong Wook YangDepartment of Systems Biology, College of Life Science and Biotechnology, Yonsei University, Seoul 03722, Republic of Korea; yangsw@yonsei.ac.kr wtkim@yonsei.ac.kr.
Woo Taek KimDepartment of Systems Biology, College of Life Science and Biotechnology, Yonsei University, Seoul 03722, Republic of Korea; yangsw@yonsei.ac.kr wtkim@yonsei.ac.kr.ORCID 0000-0001-5027-4622
Yonsei University · KRUniversity of Copenhagen · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ubiquitin E3 ligases are crucial for eliminating misfolded proteins before they form cytotoxic aggregates that threaten cell fitness and survival. However, it remains unclear how emerging misfolded proteins in the cytoplasm can be selectively recognized and eliminated by E3 ligases in plants. We found that Misfolded Protein Sensing RING E3 ligase 1 (MPSR1) is an indispensable E3 ligase required for plant survival after protein-damaging stress. Under no stress, MPSR1 is prone to rapid degradation by the 26S proteasome, concealing its protein quality control (PQC) E3 ligase activity. Upon proteotoxic stress, MPSR1 directly senses incipient misfolded proteins and tethers ubiquitins for subsequent degradation. Furthermore, MPSR1 sustains the structural integrity of the proteasome complex at the initial stage of proteotoxic stress. Here, we suggest that the MPSR1 pathway is a constitutive mechanism for proteostasis under protein-damaging stress, as a front-line surveillance system in the cytoplasm.

Indexed as

Protein FoldingProteostasisArabidopsisArabidopsis ProteinsCytoplasmDNA, PlantGene Expression Regulation, PlantGenes, PlantPhenotypeProteasome Endopeptidase ComplexProtein Interaction Domains and MotifsProteolysisRecombinant ProteinsSequence AnalysisSequence Analysis, RNAStress, PsychologicalArabidopsis ProteinsATP dependent 26S proteaseDNA, PlantProteasome Endopeptidase ComplexRecombinant ProteinsUbiquitin-Protein LigasesUbiquitinsE3 ligasePQCproteostasis

Identifiers

PMID29087340
PMCPMC5699081
OpenAlexW2766377580

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.