{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Zhao X"],"funding":["Ministry of Health and Welfare Taiwan","China Scholarship Council","Cancer Center Supporting Grant","National Science Foundation of China","Key Science and Technology Program of Shaanxi Province","Ministry of Science and Technology Taiwan","China Medical University Hospital","China Medical University","NCI NIH HHS","NIH"],"pagination":["2185-2195"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11957750"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["82(11)"],"pubmed_abstract":["Targeting immune checkpoints such as programmed cell death 1 (PD-1) and programmed cell death ligand 1 (PD-L1) has transformed cancer treatment, with durable clinical responses across a wide range of tumor types. However, a high percentage of patients fail to respond to anti-PD-1/PD-L1 treatment. A greater understanding of PD-L1 regulation is critical to improving the clinical response rate of PD-1/PD-L1 blockade. Here, we demonstrate that PD-L1 is phosphorylated and stabilized by casein kinase 2 (CK2) in cancer and dendritic cells (DC). Phosphorylation of PD-L1 at Thr285 and Thr290 by CK2 disrupted PD-L1 binding with speckle-type POZ protein, an adaptor protein of the cullin 3 (CUL3) ubiquitin E3 ligase complex, protecting PD-L1 from CUL3-mediated proteasomal degradation. Inhibition of CK"],"journal":["Cancer research"],"pubmed_title":["Phosphorylation and Stabilization of PD-L1 by CK2 Suppresses Dendritic Cell Function."],"pmcid":["PMC11957750"],"funding_grant_id":["MOHW111-TDU-B-221-114016","81903856","2021KW-60","MOST109-2314-B-039-006-MY2","82103569","2021KW-57","P30 CA016672","DMR-111-009","DMR-108-BC-6","201706280071","R01 CA208213","CMU108-YTY-02","MOST110-2639-B-039-001-ASP","R01CA208213"],"pubmed_authors":["Chan LC","Qu J","Yu D","Ying H","Zhang S","Wei Y","Chang WC","Zhao X","Jiang Z","Li Y","Chu YY","Hung MC","Yang R","Liu C","Hsu JM","Hsu JL"],"additional_accession":[]},"is_claimable":false,"name":"Phosphorylation and Stabilization of PD-L1 by CK2 Suppresses Dendritic Cell Function.","description":"Targeting immune checkpoints such as programmed cell death 1 (PD-1) and programmed cell death ligand 1 (PD-L1) has transformed cancer treatment, with durable clinical responses across a wide range of tumor types. However, a high percentage of patients fail to respond to anti-PD-1/PD-L1 treatment. A greater understanding of PD-L1 regulation is critical to improving the clinical response rate of PD-1/PD-L1 blockade. Here, we demonstrate that PD-L1 is phosphorylated and stabilized by casein kinase 2 (CK2) in cancer and dendritic cells (DC). Phosphorylation of PD-L1 at Thr285 and Thr290 by CK2 disrupted PD-L1 binding with speckle-type POZ protein, an adaptor protein of the cullin 3 (CUL3) ubiquitin E3 ligase complex, protecting PD-L1 from CUL3-mediated proteasomal degradation. Inhibition of CK","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Jun","modification":"2026-04-18T03:14:18.418Z","creation":"2025-07-10T03:08:24.511Z"},"accession":"S-EPMC11957750","cross_references":{"pubmed":["35385574"],"doi":["10.1158/0008-5472.can-21-2300","10.1158/0008-5472.CAN-21-2300"]}}