<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>12</volume><submitter>Ma XM</submitter><funding>National Natural Science Foundation of China</funding><funding>Natural Science Foundation of Guangdong Province</funding><pubmed_abstract>Immunotherapy targeting programmed death ligand-1/programmed cell death protein-1 (PD-L1/PD-1) has achieved great success in multiple cancers, but only a small subset of patients showed clinical responses. Recent evidences have shown that post-translational modification of PD-L1 protein could regulate its protein stability and interaction with cognate receptor PD-1, thereby affecting anticancer immunotherapy in several solid tumors. However, the molecular mechanisms underlying how PD-1/PD-L1 expression is regulated still remain unclear in nasopharyngeal carcinoma (NPC). Here, we found N-glycosylation of PD-L1 in NPC cells and tissues. Mechanistically, we showed that STT3A transferred N-linked glycans to PD-L1, and TGF-β1 could positively regulate STT3A expression through activating c-Jun t</pubmed_abstract><journal>Frontiers in oncology</journal><pagination>815437</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC8930841</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>TGF-β1-Mediated PD-L1 Glycosylation Contributes to Immune Escape &lt;i>via&lt;/i> c-Jun/STT3A Pathway in Nasopharyngeal Carcinoma.</pubmed_title><pmcid>PMC8930841</pmcid><pubmed_authors>Liu X</pubmed_authors><pubmed_authors>Su C</pubmed_authors><pubmed_authors>Luo YF</pubmed_authors><pubmed_authors>Li XP</pubmed_authors><pubmed_authors>Lu J</pubmed_authors><pubmed_authors>Ma XM</pubmed_authors><pubmed_authors>Zeng FF</pubmed_authors></additional><is_claimable>false</is_claimable><name>TGF-β1-Mediated PD-L1 Glycosylation Contributes to Immune Escape &lt;i>via&lt;/i> c-Jun/STT3A Pathway in Nasopharyngeal Carcinoma.</name><description>Immunotherapy targeting programmed death ligand-1/programmed cell death protein-1 (PD-L1/PD-1) has achieved great success in multiple cancers, but only a small subset of patients showed clinical responses. Recent evidences have shown that post-translational modification of PD-L1 protein could regulate its protein stability and interaction with cognate receptor PD-1, thereby affecting anticancer immunotherapy in several solid tumors. However, the molecular mechanisms underlying how PD-1/PD-L1 expression is regulated still remain unclear in nasopharyngeal carcinoma (NPC). Here, we found N-glycosylation of PD-L1 in NPC cells and tissues. Mechanistically, we showed that STT3A transferred N-linked glycans to PD-L1, and TGF-β1 could positively regulate STT3A expression through activating c-Jun t</description><dates><release>2022-01-01T00:00:00Z</release><publication>2022</publication><modification>2025-04-06T19:26:04.18Z</modification><creation>2025-04-06T19:26:04.18Z</creation></dates><accession>S-EPMC8930841</accession><cross_references><pubmed>35311117</pubmed><doi>10.3389/fonc.2022.815437</doi></cross_references></HashMap>