PRDM1 promotes the ferroptosis and immune escape of thyroid cancer by regulating USP15-mediated SELENBP1 deubiquitination
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View abstract on PubMed
Summary
This summary is machine-generated.Ubiquitin-specific peptidase 15 (USP15) promotes thyroid cancer by deubiquitinating SELENBP1. Targeting USP15 offers a potential therapeutic strategy for thyroid cancer treatment.
Area Of Science
- Oncology
- Molecular Biology
- Biochemistry
Background
- Ubiquitin-specific peptidase 15 (USP15) is implicated in various cancers, promoting tumor progression.
- USP15 upregulation is observed in thyroid cancer (TC), suggesting a role in its development.
Purpose Of The Study
- To investigate the role and underlying mechanism of USP15 in thyroid cancer progression.
- To explore the potential of USP15 as a therapeutic target in TC.
Main Methods
- Quantitative PCR and Western blot for gene and protein expression analysis.
- Cellular assays for proliferation, migration, invasion, and ferroptosis.
- In vivo xenograft models and molecular interaction studies (CoIP, ChIP, dual-luciferase reporter assays).
Main Results
- SELENBP1 upregulation in TC; its knockdown inhibited tumor growth, migration, invasion, and immune escape, while inducing ferroptosis.
- USP15 interacts with SELENBP1, stabilizing it via deubiquitination.
- PRDM1 acts as a transcription factor, inducing USP15 upregulation.
Conclusions
- USP15, transcriptionally regulated by PRDM1, promotes TC malignancy by deubiquitinating SELENBP1.
- USP15 represents a potential therapeutic target for thyroid cancer.
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