Evidence map›Paper›PMID 25792980›Full record

ArticleInternational journal of endocrinology2015

Insulin Increases Sestrin 2 Content by Reducing Its Degradation through the PI 3 K/mTOR Signaling Pathway.

Dandan Chai, Guoyu Wang, Ziyu Zhou, Hanyan Yang, Zhiwen Yu

Open access · goldAbstract read
In one paragraph

Article in International journal of endocrinology, 2015. 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
0.9field-weighted citation impact, top 26% 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, 25 citations in OpenAlex.

  1. Sestrin2 in diabetes and diabetic complications.Frontiers in endocrinology · 2023
    Review
  2. The functions and roles of sestrins in regulating human diseases.Cellular & molecular biology letters · 2022
    Review
  3. Article
  4. Article
  5. Article
  6. Sestrins in Physiological Stress Responses.Annual review of physiology · 2021
    Review
  7. Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Review
  13. The potential of sestrins as therapeutic targets for diabetes.Expert opinion on therapeutic targets · 2015
    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

5 authors at 2 institutions in 1 country.

Dandan ChaiFujian Key Laboratory of Chinese Materia Medica, Biomedical Drug Research and Development Center, Fujian University of Traditional Chinese Medicine, Fuzhou 350108, China.
Guoyu WangGuangdong Provincial Key Laboratory of Food, Nutrition and Health, Department of Nutrition, School of Public Health, Sun Yat-Sen University, Guangzhou 510080, China.
Ziyu ZhouFujian Key Laboratory of Chinese Materia Medica, Biomedical Drug Research and Development Center, Fujian University of Traditional Chinese Medicine, Fuzhou 350108, China.
Hanyan YangFujian Key Laboratory of Chinese Materia Medica, Biomedical Drug Research and Development Center, Fujian University of Traditional Chinese Medicine, Fuzhou 350108, China.
Zhiwen YuFujian Key Laboratory of Chinese Materia Medica, Biomedical Drug Research and Development Center, Fujian University of Traditional Chinese Medicine, Fuzhou 350108, China.
Fujian University of Traditional Chinese Medicine · CNSun Yat-sen University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Sestrin (SESN) is known as a cysteine sulfinic acid reductase. Recently, nonredox functions of SESN in metabolic regulation and antitumor property have been recognized. While mechanisms underlying the expression of SESN are not fully understood. Here we report that insulin markedly increased SESN2 level in HepG2 cells through mTOR activation. To determine whether insulin affects SESN2 degradation, we assessed SESN2 turnover by applying the protein synthesis inhibitor, cycloheximide (CHX), and found that following insulin treatment SESN2 protein levels were reduced significantly slower than non-insulin-treated cells. Furthermore, the proteasomal inhibitor, MG132, dramatically increased SESN2 protein and its ubiquitination level while in the presence of MG132 insulin did not further increase SESN2 content, suggesting that insulin increases SESN2 content mainly via inhibiting its proteasomal degradation. We then explored the potential feedback role of SESN2 in insulin signaling by SESN2 siRNA knockdown in HepG2 cells. Following SESN2 knockdown insulin-stimulated PKB phosphorylation was enhanced and accompanied by reduced PTEN content. Taken together, our study suggests that insulin upregulates SESN2 content via the PI3K/mTOR signaling pathway and this effect is attributed to decreased SESN2 degradation. Furthermore, SESN2 via modulating PTEN plays a negative feedback role in insulin signaling.

Identifiers

PMID25792980
PMCPMC4352509
OpenAlexW2007373141

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.