ArticleInternational journal of biological sciences2026
PTPN22 Dephosphorylates CBL to Inhibit PD-L1 Ubiquitination and Drive Immunosuppression in Renal Cell Carcinoma.
Article in International journal of biological sciences, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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2 citing papers in PubMed.
- Nanoparticle-Based delivery of proteasome inhibitors for glioblastoma Therapy: Strategies to overcome Blood-Brain barrier and therapeutic resistance.Biochemical pharmacology · 2026Review
- Integrated spatial and single‑cell transcriptomics maps disulfidptosis in renal cell carcinoma and reveals PDLIM1 as a prognostic biomarker and potential therapeutic target.Translational oncology · 2026Article
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14 authors.
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Abstract
High lymphocyte infiltration and T cell exhaustion characterize the tumor microenvironment in renal cell carcinoma (RCC). Protein tyrosine phosphatase N22 (PTPN22), a protein tyrosine phosphatase that mediates proteins tyrosine dephosphorylation, is a negative regulator of T cell receptor signaling, but its role in tumor cells has been underappreciated. PTPN22 is highly expressed in RCC cells and positively correlated with PD-L1 protein expression. CBL was newly identified as a substrate of PTPN22, and our study reveals for the first time that CBL mediates the K48-linked ubiquitination of PD-L1. PTPN22 specifically interacts with CBL, catalyzing the dephosphorylation of tyrosine 700 and inhibiting CBL binding to PD-L1, thereby preventing CBL-mediated ubiquitination and degradation of PD-L1. This stabilization of PD-L1 promotes T cell exhaustion and immunosuppression. Through screening of traditional Chinese medicine monomers, we identified curcumin as a potential PTPN22 inhibitor. Curcumin reduces PTPN22 stability and PTPN22 expression by directly binding to PTPN22.
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