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Updated: Mar 29, 2026

In Vivo Detection and Analysis of Rb Protein SUMOylation in Human Cells
Published on: November 2, 2017
USP52 impedes malignant progression and cell stemness in prostate cancer by deubiquitinating RBM5 to down-regulate
Hongliang Wu1, Sheng Wang1, Shuai Yang1
1Department of Urology, The First Affiliated Hospital of Bengbu Medical University, Bengbu, Anhui, China.
Abstract:
Ubiquitin-specific protease 52 (USP52) is vital to cancer progression by mediating the deubiquitination; however, its biological role and mechanism in prostate cancer (PCa) remain unexplored. Herein, this study aimed to discover the functional regulation of USP52 with RNA binding motif protein 5 (RBM5) and non-SMC condensin II complex subunit G2 (NCAPG2) in PCa development and stemness. RT-qPCR and Western blot were applied for expression analysis. Proliferation was assessed by colony formation and EdU assays. Cell metastasis was measured by wound healing migration assay and transwell invasion assay. Cell stemness was detected via sphere formation assay, flow analysis and Western blot detection. USP52 function in tumor growth in vivo was investigated by xenograft tumor assay. Co-immunoprecipitation was conducted for ubiquitination detection. Interaction between RBM5 and NCAPG2 was examined using dual-luciferase reporter assay. PCa samples and cells exhibited the aberrant downregulation of USP52. USP52 overexpression suppressed PCa cell proliferation, migration, invasion and stemness. PCa tumor growth in vivo was hindered by USP52. USP52 stabilized RBM5 protein expression in PCa cells by acting as a deubiquitinating enzyme. RBM5 interacted with NCAPG2 3'UTR and USP52 could down-regulate NCAPG2. USP52 repressed PCa cell progression and stemness via reducing NCAPG2. Thus, USP52 hampered PCa cell development and stemness through removing ubiquitination of RBM5 to control the expression of NCAPG2. USP52 may be used as a therapeutic target for PCa.
Insights
Ubiquitin-specific protease 52 (USP52) suppresses prostate cancer (PCa) progression and stemness by stabilizing RBM5 and reducing NCAPG2. USP52 represents a potential therapeutic target for PCa treatment.
Area of Science:
- Oncology
- Molecular Biology
- Biochemistry
Background:
- Ubiquitin-specific protease 52 (USP52) is implicated in cancer progression via deubiquitination.
- The specific role and mechanism of USP52 in prostate cancer (PCa) remain largely uncharacterized.
- Understanding USP52's regulation of key proteins like RBM5 and NCAPG2 is crucial for PCa research.
Purpose of the Study:
- To investigate the functional regulation of USP52 in prostate cancer (PCa) development and stemness.
- To elucidate the interplay between USP52, RNA binding motif protein 5 (RBM5), and non-SMC condensin II complex subunit G2 (NCAPG2) in PCa.
- To determine USP52's potential as a therapeutic target for PCa.
Main Methods:
- Quantitative reverse transcription PCR (RT-qPCR) and Western blotting for expression analysis.
- In vitro assays including proliferation (colony formation, EdU), migration (wound healing), invasion (Transwell), and stemness (sphere formation).
- In vivo xenograft tumor assays, co-immunoprecipitation for ubiquitination, and dual-luciferase reporter assays for protein interactions.
Main Results:
- USP52 was aberrantly downregulated in PCa samples and cells.
- Overexpression of USP52 significantly suppressed PCa cell proliferation, migration, invasion, and stemness, and inhibited tumor growth in vivo.
- USP52 stabilized RBM5 by deubiquitination and repressed NCAPG2 expression, thereby inhibiting PCa progression and stemness.
Conclusions:
- USP52 acts as a tumor suppressor in prostate cancer.
- USP52 inhibits PCa progression and stemness by deubiquitinating RBM5, leading to the downregulation of NCAPG2.
- USP52 demonstrates significant potential as a therapeutic target for prostate cancer.
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