Deubiquitinase USP24 activated by IL-6/STAT3 enhances PD-1 protein stability and suppresses T cell antitumor response

Authors: Hung-Chia Hsieh, Ming-Jer Young, Kuan-Yu Chen, Wu-Chou Su, Chien-Chung Lin, Yi-Ting Yen, Jan-Jong Hung, Yi-Ching Wang

Published: 2025-04-16

DOI: 10.1126/sciadv.adt4258

Source: Full article


Abstract

Persisting programmed cell death-1 (PD-1) signaling impairs T cell effector function, which is highly associated with T cell exhaustion and immunotherapy failure. However, the mechanism responsible for PD-1 deubiquitination and T cell dysfunction remains unclear. Here, we show that ubiquitin-specific peptidase 24 (USP24) promotes PD-1 protein stability by removing K48-linked polyubiquitin. Increased interleukin-6 level transcriptionally activates the USP24 expression, which leads to PD-1 stabilization. Furthermore, USP24 deficiency reduces PD-1 levels in CD8