Evidence map›Paper›PMID 34936032›Full record

ArticleCellular and molecular life sciences : CMLS2021

GSTpi reduces DNA damage and cell death by regulating the ubiquitination and nuclear translocation of NBS1.

Jinyi Zhou, Lili Gu, Yingying Shi, Ting Huang, Xirui Fan, Xiaowen Bi, Shuai Lu, Juanjuan Liang, Lan Luo, Peng Cao and 1 more

Open access · greenAbstract read
In one paragraph

Article in Cellular and molecular life sciences : CMLS, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.4field-weighted citation impact, top 39% 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

1 citing paper in PubMed, 6 citations in OpenAlex.

  1. 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

11 authors at 3 institutions in 1 country.

Jinyi Zhou *Jiangsu Province Key Laboratory for Molecular and Medical Biotechnology, College of Life Science, Nanjing Normal University, No.1 Wenyuan Road, Nanjing, 210046, People's Republic of China.ORCID http://orcid.org/0000-0002-4666-4078
Lili Gu *Jiangsu Province Key Laboratory for Molecular and Medical Biotechnology, College of Life Science, Nanjing Normal University, No.1 Wenyuan Road, Nanjing, 210046, People's Republic of China.
Yingying ShiJiangsu Province Key Laboratory for Molecular and Medical Biotechnology, College of Life Science, Nanjing Normal University, No.1 Wenyuan Road, Nanjing, 210046, People's Republic of China.
Ting HuangJiangsu Province Key Laboratory for Molecular and Medical Biotechnology, College of Life Science, Nanjing Normal University, No.1 Wenyuan Road, Nanjing, 210046, People's Republic of China.
Xirui FanJiangsu Province Key Laboratory for Molecular and Medical Biotechnology, College of Life Science, Nanjing Normal University, No.1 Wenyuan Road, Nanjing, 210046, People's Republic of China.
Xiaowen BiJiangsu Province Key Laboratory for Molecular and Medical Biotechnology, College of Life Science, Nanjing Normal University, No.1 Wenyuan Road, Nanjing, 210046, People's Republic of China.
Shuai LuJiangsu Province Key Laboratory for Molecular and Medical Biotechnology, College of Life Science, Nanjing Normal University, No.1 Wenyuan Road, Nanjing, 210046, People's Republic of China.
Juanjuan LiangJiangsu Province Key Laboratory for Molecular and Medical Biotechnology, College of Life Science, Nanjing Normal University, No.1 Wenyuan Road, Nanjing, 210046, People's Republic of China.
Lan LuoState Key Laboratory of Pharmaceutical Biotechnology, School of Life Sciences, Nanjing University, Nanjing, 210023, People's Republic of China. lanluo@nju.edu.cn.
Peng CaoAffiliated Hospital of Integrated Traditional Chinese and Western Medicine, Nanjing University of Chinese Medicine, Nanjing, People's Republic of China. cao_peng@njucm.edu.cn.
Zhimin YinJiangsu Province Key Laboratory for Molecular and Medical Biotechnology, College of Life Science, Nanjing Normal University, No.1 Wenyuan Road, Nanjing, 210046, People's Republic of China. yinzhimin@njnu.edu.cn.ORCID http://orcid.org/0000-0003-0532-7208
Nanjing Normal University · CNChina Pharmaceutical University · CNNanjing University of Chinese Medicine · CN

Funding

National Natural Science Foundation of China 31901012National Natural Science Foundation of China 32001023National Natural Science Foundation of China 81671565National Natural Science Foundation of China 81771703Postdoctoral Research Foundation of China 2020T130058ZXPriority Academic Program Development of Jiangsu Higher Education Institutions PAPD
6 · The paper itself

Abstract

Glutathione S-transferase pi (GSTpi) is an important phase II detoxifying enzyme that participates in various physiological processes, such as antioxidant, detoxification, and signal transduction. The high expression level of GSTpi has been reported to be related to drug-resistant and anti-inflammatory and it functioned via its non-catalytic ligandin. However, the previous protection mechanism of GSTpi in DNA damage has not been addressed so far. Nijmegen breakage syndrome 1 (NBS1) is one of the most important sensor proteins to detect damaged DNA. Here, we investigated the interaction between GSTpi and NBS1 in HEK-293 T cells and human breast adenocarcinoma cells during DNA damage. Our results showed that overexpression of GSTpi in cells by transfecting DNA vector decreased the DNA damage level after methyl methanesulfonate (MMS) or adriamycin (ADR) treatment. We found that cytosolic GSTpi could increase NBS1 ubiquitin-mediated degradation in unstimulated cells, which suggested that GSTpi could maintain the basal level of NBS1 during normal conditions. In response to DNA damage, GSTpi can be phosphorylated in Ser184 and inhibit the ubiquitination degradation of NBS1 mediated by Skp2 to recover NBS1 protein level. Phosphorylated GSTpi can further enhance NBS1 nuclear translocation to activate the ATM-Chk2-p53 signaling pathway. Finally, GSTpi blocked the cell cycle in the G2/M phase to allow more time for DNA damage repair. Thus, our finding revealed the novel mechanism of GSTpi via its Ser184 phosphorylation to protect cells from cell death during DNA damage and it enriches the function of GSTpi in drug resistance.

Indexed as

DNA DamageCell Cycle ProteinsGlutathione S-Transferase piHEK293 CellsHumansMCF-7 CellsNijmegen Breakage SyndromeNuclear ProteinsPhosphorylationUbiquitinationCell Cycle ProteinsGlutathione S-Transferase piGSTP1 protein, humanNBN protein, humanNuclear ProteinsDNA damage responseGSTpiNBS1Nuclear translocationUbiquitination

Identifiers

PMID34936032
PMCPMC11072236
OpenAlexW4226001455

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.