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Prothymosin‐α ( PTMA ) is a small, acidic protein that is usually transported into the nucleus and involves many cellular and immunological functions. Previous studies demonstrated that aberrant location of  PTMA  expression exists in human bladder cancer, but the role of  PTMA  protein expression remains elusive. In this study, we created ectopic nuclear or cytoplasmic  PTMA  expression in human bladder cancer cells by infecting lentiviruses carrying wild type or deleted nuclear localization signal of the   PTMA   gene. The in vivo tumorigenesis assay showed  PTMA  protein with deleted nuclear localization signal promotes J82 xenograft tumor growth in mice and shortens their survival more so than the wild type. Chromatin immunoprecipitation showed that wild‐type  PTMA  protein binds to the   PTEN   promoter and enhances phosphatase and tensin homolog ( PTEN ) expression. Through immunoblot proteomics and in vivo ubiquitination studies,  PTMA  protein can bind with tripartite motif‐containing protein 21 ( TRIM 21) and block its ubiquitination. Also,  TRIM 21 can downregulate both forms of  PTMA  protein. In human bladder tumors, loss of nuclear  PTMA  expression was an unfavorable prognostic indicator for shorter disease‐free survival (hazard ratio, 1.54;  P  = 0.009). Our data support that nuclear  PTMA  protein serves as a tumor suppressor in bladder cancer through upregulating  PTEN  and orchestrating  TRIM 21 for the regulation of Nrf2 signaling.

cancer science

Prothymosin‐α enhances phosphatase and tensin homolog expression and binds with tripartite motif‐containing protein 21 to regulate Kelch‐like ECH‐associated protein 1/nuclear factor erythroid 2‐related factor 2 signaling in human bladder cancer