Evidence map›Paper›PMID 30744690›Full record

ArticleJournal of experimental & clinical cancer research : CR2019

Nuclear accumulation of UBC9 contributes to SUMOylation of lamin A/C and nucleophagy in response to DNA damage.

Yunong Li, Xiuxing Jiang, Yanhao Zhang, Ziyi Gao, Yanxia Liu, Jinjiao Hu, Xiaoye Hu, Lirong Li, Jingshan Shi, Ning Gao

Open access · goldAbstract read
In one paragraph

Article in Journal of experimental & clinical cancer research : CR, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
2.5field-weighted citation impact, top 10% 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

47 citing papers in PubMed, 66 citations in OpenAlex.

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  19. Advances in the study of autophagy in breast cancer.Breast cancer (Tokyo, Japan) · 2024
    Review
  20. Methods to Monitor Nucleophagy in Yeast.Methods in molecular biology (Clifton, N.J.) · 2024
    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

10 authors at 3 institutions in 2 countries.

Yunong LiCollege of Pharmacy, Army Medical University, Chongqing, 400038, China.
Xiuxing JiangCollege of Pharmacy, Army Medical University, Chongqing, 400038, China.
Yanhao ZhangCollege of Pharmacy, Army Medical University, Chongqing, 400038, China.
Ziyi GaoGreater Philadelphia Pharmacy, Philadelphia, USA.
Yanxia LiuCollege of Pharmacy, Army Medical University, Chongqing, 400038, China.
Jinjiao HuCollege of Pharmacy, Army Medical University, Chongqing, 400038, China.
Xiaoye HuCollege of Pharmacy, Army Medical University, Chongqing, 400038, China.
Lirong LiCollege of Pharmacy, Army Medical University, Chongqing, 400038, China.
Jingshan ShiKey Laboratory of Basic Pharmacology of Ministry of Education and Joint International Research Laboratory of Ethnomedicine of Ministry of Education, Zunyi Medical University, Zunyi, China. shijs@zmc.edu.cn.
Ning GaoCollege of Pharmacy, Army Medical University, Chongqing, 400038, China. gaoning59@163.com.
Army Medical University · CNZunyi Medical University · CNPhiladelphia University · US

Funding

National Natural Science Foundation of China 31571425, 81402970; 81402013
6 · The paper itself

Abstract

backgroundMacroautophagy (hereafter referred to as autophagy) is an evolutionarily conserved intracellular mechanism for lysosomal degradation of damaged cellular components. The specific degradation of nuclear components by the autophagy pathway is called nucleophagy. Most studies have focused on autophagic turnover of cytoplasmic materials, and little is known about the role of autophagy in the degradation of nuclear components.

methodsHuman MDA-MB-231 and MCF-7 breast cancer cell lines were used as model systems in vitro. Induction of nucleophagy by nuclear DNA leakage was determined by western blot and immunofluorescence analyses. The interaction and colocalization of LC3 and lamin A/C was determined by immunoprecipitation and immunofluorescence. The role of the SUMO E2 ligase, UBC9, on the regulation of SUMOylation of lamin A/C and nucleophagy was determined by siRNA silencing of UBC9, and analyzed by immunoprecipitation and immunofluorescence.

resultsDNA damage induced nuclear accumulation of UBC9 ligase which resulted in SUMOylation of lamin A/C and that SUMOylation of this protein was required for the interaction between the autophagy protein LC3 and lamin A/C, which was required for nucleophagy. Knockdown of UBC9 prevented SUMOylation of lamin A/C and LC3-lamin A/C interaction. This attenuated nucleophagy which degraded nuclear components lamin A/C and leaked nuclear DNA mediated by DNA damage.

conclusionsOur findings suggest that nuclear DNA leakage activates nucleophagy through UBC9-mediated SUMOylation of lamin A/C, leading to degradation of nuclear components including lamin A/C and leaked nuclear DNA.

Indexed as

DNA DamageA549 CellsAutophagyBreast NeoplasmsCell Line, TumorCell NucleusDoxorubicinHEK293 CellsHep G2 CellsHumansLaminsLamin Type AMCF-7 CellsMicroscopy, ConfocalSumoylationUbiquitin-Conjugating EnzymesDoxorubicinlamin C protein, humanLaminsLamin Type AUbiquitin-Conjugating EnzymesUbiquitin-Conjugating Enzyme UBC9Lamin A/CLC3NucleophagySUMOylationUBC9

Identifiers

PMID30744690
PMCPMC6371487
OpenAlexW2922237706

What OpenQuestion holds

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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.