Evidence map›Paper›PMID 36878903›Full record

ArticleCell death & disease2023

USP7- and PRMT5-dependent G3BP2 stabilization drives de novo lipogenesis and tumorigenesis of HNSC.

Nan Wang, Tianzi Li, Wanyu Liu, Jinhua Lin, Ke Zhang, Zhenhao Li, Yanfei Huang, Yufei Shi, Meilan Xu, Xuekui Liu

Open access · goldAbstract read
In one paragraph

Article in Cell death & disease, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
6.0field-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

16 citing papers in PubMed, 39 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Review
  6. Review
  7. Article
  8. Review
  9. Article
  10. Article
  11. Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. 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 2 institutions in 1 country.

Nan WangLaboratory of Cell and Molecular Biology, School of life sciences, Jiaying University, Meizhou, China. wangnan@jyu.edu.cn.ORCID 0000-0002-3413-1450
Tianzi LiLaboratory of Cell and Molecular Biology, School of life sciences, Jiaying University, Meizhou, China.
Wanyu LiuLaboratory of Cell and Molecular Biology, School of life sciences, Jiaying University, Meizhou, China.
Jinhua LinLaboratory of Cell and Molecular Biology, School of life sciences, Jiaying University, Meizhou, China.
Ke ZhangLaboratory of Cell and Molecular Biology, School of life sciences, Jiaying University, Meizhou, China.
Zhenhao LiLaboratory of Cell and Molecular Biology, School of life sciences, Jiaying University, Meizhou, China.
Yanfei HuangLaboratory of Cell and Molecular Biology, School of life sciences, Jiaying University, Meizhou, China.
Yufei ShiLaboratory of Cell and Molecular Biology, School of life sciences, Jiaying University, Meizhou, China.
Meilan XuLaboratory of Cell and Molecular Biology, School of life sciences, Jiaying University, Meizhou, China.
Xuekui LiuState Key Laboratory of Oncology in South China, Collaborative Innovation Center for Cancer Medicine, Sun Yat-sen University Cancer Center, Guangzhou, China.ORCID 0000-0002-6635-1095
Jiaying University · CNSun Yat-sen University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

GTPase-activating protein-binding protein 2 (G3BP2) is a key stress granule-associated RNA-binding protein responsible for the formation of stress granules (SGs). Hyperactivation of G3BP2 is associated with various pathological conditions, especially cancers. Emerging evidence indicates that post-translational modifications (PTMs) play critical roles in gene transcription, integrate metabolism and immune surveillance. However, how PTMs directly regulate G3BP2 activity is lacking. Here, our analyses identify a novel mechanism that PRMT5-mediated G3BP2-R468me2 enhances the binding to deubiquitinase USP7, which ensures the deubiquitination and stabilization of G3BP2. Mechanistically, USP7- and PRMT5-dependent G3BP2 stabilization consequently guarantee robust ACLY activation, which thereby stimulating de novo lipogenesis and tumorigenesis. More importantly, USP7-induced G3BP2 deubiquitination is attenuated by PRMT5 depletion or inhibition. PRMT5-activity dependent methylation of G3BP2 is required for its deubiquitination and stabilization by USP7. Consistently, G3BP2, PRMT5 and G3BP2 R468me2 protein levels were found positively correlated in clinical patients and associated with poor prognosis. Altogether, these data suggest that PRMT5-USP7-G3BP2 regulatory axis serves as a lipid metabolism reprogramming mechanism in tumorigenesis, and unveil a promising therapeutic target in the metabolic treatment of head and neck squamous carcinoma.

Indexed as

Head and Neck NeoplasmsLipogenesisAdaptor Proteins, Signal TransducingCarcinogenesisCell Transformation, NeoplasticHumansProtein-Arginine N-MethyltransferasesRNA-Binding ProteinsUbiquitin-Specific Peptidase 7Adaptor Proteins, Signal TransducingG3BP2 protein, humanPRMT5 protein, humanProtein-Arginine N-MethyltransferasesRNA-Binding ProteinsUbiquitin-Specific Peptidase 7USP7 protein, human

Identifiers

PMID36878903
PMCPMC9988876
OpenAlexW4323310514

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.