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Proanthocyanidins enhance antitumor immunity by promoting ubiquitin-proteasomal PD-L1 degradation via stabilization of LKB1 and SYVN1
Mengting Xu, Xuwen Lin, Hanchi Xu, Hongmei Hu, Xinying Xue, Qing Zhang, Dianping Yu, Saisai Tian, Mei Xie, Linyang Li, Xiaoyu Tao, Xinru Li, Simeng Li, Shize Xie, Yating Tian, Xia Liu, Hanchen Xu, Qun Wang, Weidong Zhang, Sanhong Liu
Mengting Xu, Xuwen Lin, Hanchi Xu, Hongmei Hu, Xinying Xue, Qing Zhang, Dianping Yu, Saisai Tian, Mei Xie, Linyang Li, Xiaoyu Tao, Xinru Li, Simeng Li, Shize Xie, Yating Tian, Xia Liu, Hanchen Xu, Qun Wang, Weidong Zhang, Sanhong Liu
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Research Article Immunology Oncology

Proanthocyanidins enhance antitumor immunity by promoting ubiquitin-proteasomal PD-L1 degradation via stabilization of LKB1 and SYVN1

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Abstract

Programmed cell death 1 ligand 1–targeted (PD-L1–targeted) immune checkpoint inhibitors are revolutionizing cancer therapy. However, strategies to induce endogenous PD-L1 degradation represent an emerging therapeutic paradigm. Here, we identified proanthocyanidins (PC) as a potent inducer of PD-L1 degradation through an endoplasmic reticulum–associated degradation (ERAD) mechanism. Mechanistically, PC exerted dual effects: First, it targeted and stabilized LKB1 to activate AMPK in tumor cells, subsequently inducing the phosphorylation of PD-L1 at Ser195 — a disruption that in turn impaired glycosylation of PD-L1 and promoted its retention in the ER. Second, PC directly bound to the E3 ubiquitin ligase SYVN1 to increase its protein stability, which strengthened PD-L1–SYVN1 binding, thereby accelerating K48-linked ubiquitination and proteasomal degradation of ER-retained PD-L1. This cascade culminated in the activation of CD8+ T cell–dominated antitumor immune responses, accompanied by suppression of myeloid-derived suppressor cells and regulatory T cells. In preclinical models of lung and colorectal cancer, PC exhibited synergistic antitumor efficacy when combined with anti–cytotoxic T lymphocyte antigen 4 (anti–CTLA-4) antibodies. Notably, PC also potently inhibited the progression of azoxymethane/dextran sodium sulfate–induced orthotopic colorectal cancer in mice. Collectively, our findings unveil an antitumor mechanism of PC, establishing this small-molecule compound as an ERAD pathway–exploiting immune checkpoint modulator with promising translational potential for cancer therapy.

Authors

Mengting Xu, Xuwen Lin, Hanchi Xu, Hongmei Hu, Xinying Xue, Qing Zhang, Dianping Yu, Saisai Tian, Mei Xie, Linyang Li, Xiaoyu Tao, Xinru Li, Simeng Li, Shize Xie, Yating Tian, Xia Liu, Hanchen Xu, Qun Wang, Weidong Zhang, Sanhong Liu

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Figure 8

PC targets LKB1 to activate AMPK phosphorylation and downregulate PD-L1.

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PC targets LKB1 to activate AMPK phosphorylation and downregulate PD-L1....
(A) RKO cells were pretreated with 10 μM compound C dihydrochloride (CCd) (10 μM) or vehicle (2 hours), then 30 μM PC (9 hours). Immunoblotting for p-AMPKα (Thr172), AMPKα, PD-L1. (B) Western blot analysis of RKO cells treated with Pim1 (5, 10 μM; 2 hours) ± 30 μM PC (9 hours) for p-AMPKα (Thr172), AMPKα, LKB1, and PD-L1. (C) RKO cells were cotreated with CHX and PC or vehicle, and the LKB1 half-life was assessed by Western blotting. (D) LKB1 mRNA levels in RKO cells after 40 μM PC treatment for 9 hours (RT-qPCR). (E) CETSA was used to evaluate PC-induced thermal stabilization of LKB1 across a range of temperatures. (F and G) LKB1 thermal stability at 42°C under increasing PC concentrations and quantification of these results. (H and I) LKB1 proteolytic susceptibility was assessed by DARTS assay at PC-to-protein ratios of 1:400 (H), with quantification shown in I. (J and K) Molecular docking simulations illustrating potential binding modes between PC and LKB1. (L–N) MST analysis of the interaction between PC and GFP-tagged WT LKB1 (L) or its mutants (Asp141A, Ser428A) (M and N). (O) RKO cells expressing GFP-tagged WT or mutant LKB1 (Asp141A, Ser428A) were treated with or without 30 μM PC for 9 hours, followed by a 24-hour coculture with PHA/PMA-activated Jurkat T cells at a 9:1 ratio. Surviving cells were quantified by crystal violet staining and Cytation 5 imaging. (P) The quantitative plot of O. The data shown are the mean ± SEM. Statistical differences were determined by unpaired 2-tailed Student’s t test (D), 2-way ANOVA with Šídák multiple comparisons test (E), and 1-way ANOVA with Dunnett multiple comparisons test (all other panels). *P < 0.05, and ****P < 0.0001.

Copyright © 2026 American Society for Clinical Investigation
ISSN: 0021-9738 (print), 1558-8238 (online)

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