Evidence map›Paper›PMID 40990019›Full record

ReviewFrontiers in immunology2025

USP39 at the crossroads of cancer immunity: regulating immune evasion and immunotherapy response through RNA splicing and ubiquitin signaling.

Feilong Zhou, Xinhao Li, Yanmei Sun, Yizhu Wang, Kaiyi Niu, Xin Gao, Jiaqi Zhang, Tianyi Chen, Yunxin Li, Weijie Zhao and 4 more

Abstract readReview
In one paragraph

Review in Frontiers in immunology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
–field-weighted citation impact
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

3 citing papers in PubMed.

  1. Ubiquitination and NOncology letters · 2026
    Review
  2. Article
  3. 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

14 authors.

Feilong Zhou *General Surgery Department, The Second Affiliated Hospital of Nanjing Medical University, Nanjing, China.
Xinhao Li *General Surgery Department, The Second Affiliated Hospital of Nanjing Medical University, Nanjing, China.
Yanmei Sun *General Surgery Department, The Second Affiliated Hospital of Nanjing Medical University, Nanjing, China.
Yizhu Wang *General Surgery Department, The Second Affiliated Hospital of Nanjing Medical University, Nanjing, China.
Kaiyi NiuGeneral Surgery Department, The Second Affiliated Hospital of Nanjing Medical University, Nanjing, China.
Xin GaoGeneral Surgery Department, The Second Affiliated Hospital of Nanjing Medical University, Nanjing, China.
Jiaqi ZhangGeneral Surgery Department, The Second Affiliated Hospital of Nanjing Medical University, Nanjing, China.
Tianyi ChenGeneral Surgery Department, The Second Affiliated Hospital of Nanjing Medical University, Nanjing, China.
Yunxin LiGeneral Surgery Department, The Second Affiliated Hospital of Nanjing Medical University, Nanjing, China.
Weijie ZhaoGeneral Surgery Department, The Second Affiliated Hospital of Nanjing Medical University, Nanjing, China.
Binyue MaoDepartment of Dermatology, The First Affiliated Hospital of Xi'an Jiaotong University, Xi'an, China.
Qiyang XuGeneral Surgery Department, Fuyang Fifth People's Hospital, Fuyang, China.
Yanlong ShiGeneral Surgery Department, Fuyang Hospital of Anhui Medical University, Fuyang, China.
Zhenyu HeGeneral Surgery Department, The Second Affiliated Hospital of Nanjing Medical University, Nanjing, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Deubiquitinating enzymes (DUBs) are responsible for the removal of ubiquitin from substrates, thereby antagonizing ubiquitination and regulating a multitude of biological pathways including cell cycle progression, signal transduction, and transcriptional regulation. Ubiquitin Specific Protease-39 (USP39), a pivotal member of the ubiquitin-specific protease family, is intricately linked to innumerable pathophysiological processes. In this review, we first provide an overview of the specific structural domains and biological functions of USP39, with a particular focus on its role in DNA damage repair and RNA splicing processes. Then, we delineate the function of USP39 in maintaining epithelial morphology, resistance to viral infection, vascular remodeling, and pathological states. Moreover, we particularly focus on the aberrant expression of USP39 in various cancers and its effect on cancer markers, as well as on the regulatory role of USP39 in tumor progression. In conclusion, a comprehensive analysis of the structural domains and functional properties of USP39, a detailed investigation into its interaction mechanisms with diverse substrates, and the accelerated development of related inhibitors will provide a novel theoretical foundation for the treatment of numerous diseases, including tumors. Importantly, targeting USP39 may overcome resistance to checkpoint inhibitors, offering a promising approach to enhance cancer immunotherapy efficacy.

Indexed as

Immune EvasionNeoplasmsRNA SplicingTumor EscapeUbiquitinUbiquitin-Specific ProteasesAnimalsHumansImmunotherapySignal TransductionUbiquitinationUbiquitinUbiquitin-Specific ProteasesUSP39 protein, humancancersdeubiquitylationDNA damage repairimmunotherapyregulationRNA splicingstructureUSP39

Identifiers

PMID40990019
PMCPMC12450694

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.