Evidence map›Paper›PMID 40319028›Full record

ArticleCell death & disease2025

TSPYL5-driven G3BP1 nuclear membrane translocation facilitates p53 cytoplasm sequestration via accelerating RanBP2-mediated p53 sumoylation and nuclear export in neuroblastoma.

Zhaokun Wang, Yunqiang Liu, Yangwei Zhang, Jiaying Shi, Shengyu Xie, Ming Yi, Xinyue Zhang, Dachang Tao, Yuan Yang

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Cell death & disease, 2025. 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
–field-weighted citation impact
1 · What the graph read from it

What it found

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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

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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.

  1. Review
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

9 authors.

Zhaokun Wang *Department of Medical Genetics, State Key Laboratory of Biotherapy, West China Hospital, Sichuan University, Chengdu, China.
Yunqiang Liu *Department of Medical Genetics, State Key Laboratory of Biotherapy, West China Hospital, Sichuan University, Chengdu, China.
Yangwei Zhang *Department of Medical Genetics, State Key Laboratory of Biotherapy, West China Hospital, Sichuan University, Chengdu, China.
Jiaying ShiDepartment of Medical Genetics, State Key Laboratory of Biotherapy, West China Hospital, Sichuan University, Chengdu, China.
Shengyu XieDepartment of Medical Genetics, State Key Laboratory of Biotherapy, West China Hospital, Sichuan University, Chengdu, China.
Ming YiDepartment of Medical Genetics, State Key Laboratory of Biotherapy, West China Hospital, Sichuan University, Chengdu, China.
Xinyue ZhangDepartment of Medical Genetics, State Key Laboratory of Biotherapy, West China Hospital, Sichuan University, Chengdu, China.
Dachang TaoDepartment of Medical Genetics, State Key Laboratory of Biotherapy, West China Hospital, Sichuan University, Chengdu, China.
Yuan YangDepartment of Medical Genetics, State Key Laboratory of Biotherapy, West China Hospital, Sichuan University, Chengdu, China. yangyuan@scu.edu.cn.ORCID http://orcid.org/0000-0002-9206-0312

Funding

National Natural Science Foundation of China (National Science Foundation of China) 81871203
6 · The paper itself

Abstract

Cytoplasmic sequestration of wild-type p53, representing a nonmutational event of p53 activity suppression, is a characteristic phenotype of undifferentiated neuroblastoma (NB); however, the underlying mechanism is yet to be defined. In the present study, we observed that TSPYL5 effectively tethers p53 in the cytoplasm and greatly inhibits its function as a transcription factor. Mechanistically, the binding of TSPYL5 with G3BP1 enhances G3BP1 Ser149 phosphorylation to drive G3BP1 nuclear membrane translocation, which recruits more p53 for nucleoporin RanBP2 by the formation of the RanBP2-G3BP1-p53 complex. Thus, the accelerating p53 sumoylation promotes its nuclear export. With this signal pathway, TSPYL5 augments the malignant characteristics of neuroblastoma cells. Our findings unravel a detailed TSPYL5-driven molecular axis that sheds light on the regulating system of the p53 sumoylation-based cytoplasmic sequestration in NB cells, paving the way for the novel therapeutic opportunities for NB cancers by antagonizing TSPYL5 function.

Indexed as

CytoplasmDNA HelicasesMolecular ChaperonesNeuroblastomaNuclear EnvelopeNuclear Pore Complex ProteinsPoly-ADP-Ribose Binding ProteinsRNA Recognition Motif ProteinsTumor Suppressor Protein p53Active Transport, Cell NucleusCell Line, TumorCell NucleusHumansPhosphorylationRNA HelicasesSumoylationDNA HelicasesG3BP1 protein, humanMolecular ChaperonesNuclear Pore Complex ProteinsPoly-ADP-Ribose Binding Proteinsran-binding protein 2RNA HelicasesRNA Recognition Motif ProteinsTP53 protein, humanTumor Suppressor Protein p53

Identifiers

PMID40319028
PMCPMC12049415

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