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<p>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.</p>

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USP52 impedes malignant progression and cell stemness in prostate cancer by deubiquitinating RBM5 to down-regulate NCAPG2

  • 期刊论文

  • 发表日期：

    2026年3月27日

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  • Hongliang Wu,
  • Sheng Wang,
  • Shuai Yang,
  • Wenyan Sun,
  • Han Guan

摘要

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.