Evidence map›Paper›PMID 31483571›Full record

ArticleJournal of integrative plant biology2020

AtSec62 is critical for plant development and is involved in ER-phagy in Arabidopsis thaliana.

Shuai Hu, Hao Ye, Yong Cui, Liwen Jiang

Open access · hybridAbstract read
In one paragraph

Article in Journal of integrative plant biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed, 1 pooled it
5.6field-weighted citation impact, top 3% 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

54 citing papers in PubMed, 1 synthesis or guideline pooled it, 90 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Review
  4. Review
  5. Review
  6. Review
  7. Article
  8. Article
  9. Visualizing ER-phagy and ER architecture in vivo.The Journal of cell biology · 2024
    Article
  10. Review
  11. Review
  12. Review
  13. An Overview of Protein Secretion in Plant Cells.Methods in molecular biology (Clifton, N.J.) · 2024
    Review
  14. Autophagy in plants.Autophagy reports · 2024
    Review
  15. Mechanisms of Endoplasmic Reticulum Protein Homeostasis in Plants.International journal of molecular sciences · 2023
    Review
  16. The Time-Resolved Salt Stress Response ofInternational journal of molecular sciences · 2023
    Article
  17. Article
  18. Article
  19. Article
  20. Review
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.

Shuai HuCentre for Cell & Developmental Biology and State Key Laboratory of Agrobiotechnology, School of Life Sciences, The Chinese University of Hong Kong, Hong Kong, China.
Hao YeCentre for Cell & Developmental Biology and State Key Laboratory of Agrobiotechnology, School of Life Sciences, The Chinese University of Hong Kong, Hong Kong, China.
Yong CuiCentre for Cell & Developmental Biology and State Key Laboratory of Agrobiotechnology, School of Life Sciences, The Chinese University of Hong Kong, Hong Kong, China.
Liwen JiangCentre for Cell & Developmental Biology and State Key Laboratory of Agrobiotechnology, School of Life Sciences, The Chinese University of Hong Kong, Hong Kong, China.
Chinese University of Hong Kong · CN

Funding

CUHK Research CommitteeNational Natural Science Foundation of ChinaResearch Grants Council of Hong Kong
6 · The paper itself

Abstract

The endoplasmic reticulum (ER) is the major site for protein folding in eukaryotic cells. ER homeostasis is essential for the development of an organism, whereby the unfolded protein response (UPR) within the ER is precisely regulated. ER-phagy is a newly identified selective autophagic pathway for removal of misfolded or unfolded proteins within the ER in mammalian cells. Sec62, a component of the translocon complex, was recently characterized as an ER-phagy receptor during the ER stress recovery phase in mammals. In this study, we demonstrated that the Arabidopsis Sec62 (AtSec62) is required for plant development and might function as an ER-phagy receptor in plants. We showed that AtSec62 is an ER-localized membrane protein with three transmembrane domains (TMDs) with its C-terminus facing to the ER lumen. AtSec62 is required for plant development because atsec62 mutants display impaired vegetative growth, abnormal pollen and decreased fertility. atsec62 mutants are sensitive towards tunicamycin (TM)-induced ER stress, whereas overexpression of AtSec62 subsequently enhances stress tolerance during the ER stress recovery phase. Moreover, YFP-AtSec62 colocalizes with the autophagosome marker mCh-Atg8e in ring-like structures upon ER stress induction. Taken together, these data provide evidence for the pivotal roles of AtSec62 in plant development and ER-phagy.

Indexed as

ArabidopsisArabidopsis ProteinsEndoplasmic ReticulumEndoplasmic Reticulum StressTunicamycinUnfolded Protein ResponseArabidopsis ProteinsTunicamycin

Identifiers

PMID31483571
PMCPMC7028082
OpenAlexW2971834059

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.