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Title:
NEK2 inhibition triggers anti-pancreatic cancer immunity by targeting PD-L1 | Nature Communications
Description:
Despite the substantial impact of post-translational modifications on programmed cell death 1 ligand 1 (PD-L1), its importance in therapeutic resistance in pancreatic cancer remains poorly defined. Here, we demonstrate that never in mitosis gene A-related kinase 2 (NEK2) phosphorylates PD-L1 to maintain its stability, causing PD-L1-targeted pancreatic cancer immunotherapy to have poor efficacy. We identify NEK2 as a prognostic factor in immunologically βhotβ pancreatic cancer, involved in the onset and development of pancreatic tumors in an immune-dependent manner. NEK2 deficiency results in the suppression of PD-L1 expression and enhancement of lymphocyte infiltration. A NEK binding motif (F/LXXS/T) is identified in the glycosylation-rich region of PD-L1. NEK2 interacts with PD-L1, phosphorylating the T194/T210 residues and preventing ubiquitin-proteasome pathway-mediated degradation of PD-L1 in ER lumen. NEK2 inhibition thereby sensitizes PD-L1 blockade, synergically enhancing the anti-pancreatic cancer immune response. Together, the present study proposes a promising strategy for improving the effectiveness of pancreatic cancer immunotherapy. NEK2 is a serine-threonine kinase overexpressed in a variety of human cancers. Here the authors show that NEK2 controls the stability of PD-L1 by preventing its proteasome-mediated degradation and that NEK2 targeting restores anti-tumor immune responses in preclinical models of pancreatic cancer.
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nature portfolio privacy policy anti-phospho-t194/t210-pd-l1 antibodies advertising pe/cy7 anti-human cd11b sensitizing pd-l1-targeted therapy apc/cy7 anti-human cd11c cell-mediated tumor cell-destruction pd-1/pd-l1-targeted immunotherapy mono-anti-pd-l1 antibody profiling service apc/cy7 anti-mouse cd3 middle line mediated pd-l1 poly-ubiquitination pe/cy7 anti-mouse cd8a national key research invivomab anti-mouse pd-l1 social media source data file apc anti-mouse tnf-Ξ± regulates anti-tumour immunity myeloid-derived suppressor cells large-scale rna-seq datasets pd-1/pd-l1 signaling axis fitc anti-mouse ifn-Ξ³ e3 ubiquitin-protein ligase nek2βpd-l1 signaling pathway sensitizes pd-l1 blockade reprints anti-pd-1/pd-l1 therapy t194/t210-pd-l1 peptide nature 553 nature 548 nature 549 nature goat anti-rabbit igg pd-l1-based combinatorial therapy t193/209d-transfected kpc cells key research anti-mouse cd16/32 antibody pd-l1-targeted drugs bv785 anti-human cd45 goat anti-mouse igg stabilizes d-type cyclins anti-phospho-gsk-3Ξ² 6-ethynyl-9h-purin-2-yl experimental animal center real-time quantitative pcr hrp-conjugated secondary antibody apc anti-human cd15
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headline:NEK2 inhibition triggers anti-pancreatic cancer immunity by targeting PD-L1
description:Despite the substantial impact of post-translational modifications on programmed cell death 1 ligand 1 (PD-L1), its importance in therapeutic resistance in pancreatic cancer remains poorly defined. Here, we demonstrate that never in mitosis gene A-related kinase 2 (NEK2) phosphorylates PD-L1 to maintain its stability, causing PD-L1-targeted pancreatic cancer immunotherapy to have poor efficacy. We identify NEK2 as a prognostic factor in immunologically Γ’ΒΒhotΓ’ΒΒ pancreatic cancer, involved in the onset and development of pancreatic tumors in an immune-dependent manner. NEK2 deficiency results in the suppression of PD-L1 expression and enhancement of lymphocyte infiltration. A NEK binding motif (F/LXXS/T) is identified in the glycosylation-rich region of PD-L1. NEK2 interacts with PD-L1, phosphorylating the T194/T210 residues and preventing ubiquitin-proteasome pathway-mediated degradation of PD-L1 in ER lumen. NEK2 inhibition thereby sensitizes PD-L1 blockade, synergically enhancing the anti-pancreatic cancer immune response. Together, the present study proposes a promising strategy for improving the effectiveness of pancreatic cancer immunotherapy. NEK2 is a serine-threonine kinase overexpressed in a variety of human cancers. Here the authors show that NEK2 controls the stability of PD-L1 by preventing its proteasome-mediated degradation and that NEK2 targeting restores anti-tumor immune responses in preclinical models of pancreatic cancer.
datePublished:2021-07-27T00:00:00Z
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Pancreatic cancer
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multidisciplinary
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headline:NEK2 inhibition triggers anti-pancreatic cancer immunity by targeting PD-L1
description:Despite the substantial impact of post-translational modifications on programmed cell death 1 ligand 1 (PD-L1), its importance in therapeutic resistance in pancreatic cancer remains poorly defined. Here, we demonstrate that never in mitosis gene A-related kinase 2 (NEK2) phosphorylates PD-L1 to maintain its stability, causing PD-L1-targeted pancreatic cancer immunotherapy to have poor efficacy. We identify NEK2 as a prognostic factor in immunologically Γ’ΒΒhotΓ’ΒΒ pancreatic cancer, involved in the onset and development of pancreatic tumors in an immune-dependent manner. NEK2 deficiency results in the suppression of PD-L1 expression and enhancement of lymphocyte infiltration. A NEK binding motif (F/LXXS/T) is identified in the glycosylation-rich region of PD-L1. NEK2 interacts with PD-L1, phosphorylating the T194/T210 residues and preventing ubiquitin-proteasome pathway-mediated degradation of PD-L1 in ER lumen. NEK2 inhibition thereby sensitizes PD-L1 blockade, synergically enhancing the anti-pancreatic cancer immune response. Together, the present study proposes a promising strategy for improving the effectiveness of pancreatic cancer immunotherapy. NEK2 is a serine-threonine kinase overexpressed in a variety of human cancers. Here the authors show that NEK2 controls the stability of PD-L1 by preventing its proteasome-mediated degradation and that NEK2 targeting restores anti-tumor immune responses in preclinical models of pancreatic cancer.
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Pancreatic cancer
Tumour immunology
Science
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multidisciplinary
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