Evidence map›Paper›PMID 24496447›Full record

ArticleJournal of cell science2014

Ube2g2-gp78-mediated HERP polyubiquitylation is involved in ER stress recovery.

Long Yan, Weixiao Liu, Huihui Zhang, Chao Liu, Yongliang Shang, Yihong Ye, Xiaodong Zhang, Wei Li

Open access · greenAbstract read
In one paragraph

Article in Journal of cell science, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.3field-weighted citation impact, top 13% 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

22 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
  2. Article
  3. The role of ubiquitin-conjugating enzyme in the process of spermatogenesis.Reproductive biology and endocrinology : RB&E · 2024
    Review
  4. Review
  5. Endoplasmic Reticulum-Associated Protein Degradation.Cold Spring Harbor perspectives in biology · 2022
    Review
  6. Article
  7. Review
  8. Article
  9. TheProceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Review
  18. Article
  19. Review
  20. 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

8 authors at 4 institutions in 2 countries.

Long YanState Key Laboratory of Reproductive Biology, Institute of Zoology, Chinese Academy of Sciences, Beijing 100101, China.
Weixiao Liu
Huihui Zhang
Chao Liu
Yongliang Shang
Yihong Ye
Xiaodong Zhang
Wei Li
Institute of Zoology · CNChinese Academy of Sciences · CNWuhan University · CNNational Institute of Diabetes and Digestive and Kidney Diseases · US

Funding

Mechanism of protein retro-translocation from the endoplasmic reticulumZIADK033008 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI YE, YIHONG · 2010 to 2025
$9.3M
Mechanism of polyubiquitin chain assembly by an ER-associated ubiquitin ligaseZIADK036137 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI YE, YIHONG · 2009 to 2014
$486k
Intramural NIH HHS
6 · The paper itself

Abstract

A large number of studies have focused on how individual organisms respond to a stress condition, but little attention has been paid to the stress recovery process, such as the endoplasmic reticulum (ER) stress recovery. Homocysteine-induced ER protein (HERP) was originally identified as a chaperone-like protein that is strongly induced upon ER stress. Here we show that, after ER stress induction, HERP is rapidly degraded by Ube2g2-gp78-mediated ubiquitylation and proteasomal degradation. The polyubiquitylation of HERP in vitro depends on a physical interaction between the CUE domain of gp78 and the ubiquitin-like (UBL) domain of HERP, which is essential for HERP degradation in vivo during ER stress recovery. We further show that although HERP promotes cell survival under ER stress, high levels of HERP expression reduce cell viability under oxidative stress conditions, suggesting that HERP plays a dual role in cellular stress adaptation. Together, these results establish the ubiquitin-proteasome-mediated degradation of HERP as a novel mechanism that fine-tunes the stress tolerance capacity of the cell.

Indexed as

AnimalsCells, CulturedEndoplasmic Reticulum StressHumansMembrane ProteinsMiceUbiquitinationUbiquitin-Conjugating EnzymesHERPUD1 protein, humanHerpud1 protein, mouseMembrane ProteinsUBE2G2 protein, humanUBE2G2 protein, mouseUbiquitin-Conjugating EnzymesER Stress recoveryHERPTrade-offUbe2g2–gp78Ubiquitin–proteasome system

Identifiers

PMID24496447
PMCPMC4074213
OpenAlexW2105777060

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.