ARIH1 activates STING-mediated T-cell activation and sensitizes tumors to immune checkpoint blockade

Nat Commun. 2023 Jul 10;14(1):4066. doi: 10.1038/s41467-023-39920-5.

Abstract

Despite advances in cancer treatment, immune checkpoint blockade (ICB) only achieves complete response in some patients, illustrating the need to identify resistance mechanisms. Using an ICB-insensitive tumor model, here we discover cisplatin enhances the anti-tumor effect of PD-L1 blockade and upregulates the expression of Ariadne RBR E3 ubiquitin-protein ligase 1 (ARIH1) in tumors. Arih1 overexpression promotes cytotoxic T cell infiltration, inhibits tumor growth, and potentiates PD-L1 blockade. ARIH1 mediates ubiquitination and degradation of DNA-PKcs to trigger activation of the STING pathway, which is blocked by the phospho-mimetic mutant T68E/S213D of cGAS protein. Using a high-throughput drug screen, we further identify that ACY738, less cytotoxic than cisplatin, effectively upregulates ARIH1 and activates STING signaling, sensitizing tumors to PD-L1 blockade. Our findings delineate a mechanism that tumors mediate ICB resistance through the loss of ARIH1 and ARIH1-DNA-PKcs-STING signaling and indicate that activating ARIH1 is an effective strategy to improve the efficacy of cancer immunotherapy.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • B7-H1 Antigen* / genetics
  • Cisplatin / pharmacology
  • Cisplatin / therapeutic use
  • DNA
  • Humans
  • Immune Checkpoint Inhibitors / pharmacology
  • Immune Checkpoint Inhibitors / therapeutic use
  • Neoplasms* / drug therapy
  • T-Lymphocytes
  • Ubiquitin-Protein Ligases / genetics

Substances

  • B7-H1 Antigen
  • Cisplatin
  • Immune Checkpoint Inhibitors
  • DNA
  • ARIH1 protein, human
  • Ubiquitin-Protein Ligases