Glycosylation and stabilization of programmed death ligand-1 suppresses T-cell activity View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2016-08-30

AUTHORS

Chia-Wei Li, Seung-Oe Lim, Weiya Xia, Heng-Huan Lee, Li-Chuan Chan, Chu-Wei Kuo, Kay-Hooi Khoo, Shih-Shin Chang, Jong-Ho Cha, Taewan Kim, Jennifer L. Hsu, Yun Wu, Jung-Mao Hsu, Hirohito Yamaguchi, Qingqing Ding, Yan Wang, Jun Yao, Cheng-Chung Lee, Hsing-Ju Wu, Aysegul A. Sahin, James P. Allison, Dihua Yu, Gabriel N. Hortobagyi, Mien-Chie Hung

ABSTRACT

Extracellular interaction between programmed death ligand-1 (PD-L1) and programmed cell death protein-1 (PD-1) leads to tumour-associated immune escape. Here we show that the immunosuppression activity of PD-L1 is stringently modulated by ubiquitination and N-glycosylation. We show that glycogen synthase kinase 3β (GSK3β) interacts with PD-L1 and induces phosphorylation-dependent proteasome degradation of PD-L1 by β-TrCP. In-depth analysis of PD-L1 N192, N200 and N219 glycosylation suggests that glycosylation antagonizes GSK3β binding. In this regard, only non-glycosylated PD-L1 forms a complex with GSK3β and β-TrCP. We also demonstrate that epidermal growth factor (EGF) stabilizes PD-L1 via GSK3β inactivation in basal-like breast cancer. Inhibition of EGF signalling by gefitinib destabilizes PD-L1, enhances antitumour T-cell immunity and therapeutic efficacy of PD-1 blockade in syngeneic mouse models. Together, our results link ubiquitination and glycosylation pathways to the stringent regulation of PD-L1, which could lead to potential therapeutic strategies to enhance cancer immune therapy efficacy. More... »

PAGES

12632

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/ncomms12632

DOI

http://dx.doi.org/10.1038/ncomms12632

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1038663513

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/27572267


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