Inhibiting PD-L1 palmitoylation enhances T-cell immune responses in opposition to tumours


Brahmer, J. R. et al. Security and exercise of anti-PD-L1 antibody in sufferers with superior most cancers. N. Engl. J. Med. 366, 2455–2465 (2012).


Sonpavde, G. PD-1 and PD-L1 inhibitors as salvage remedy for urothelial carcinoma. N. Engl. J. Med. 376, 1073–1074 (2017).


Yao, H., Wang, H., Li, C., Fang, J. Y. & Xu, J. Most cancers cell-intrinsic PD-1 and implications in combinatorial immunotherapy. Entrance. Immunol. 9, 1774 (2018).


Rodell, C. B. et al. TLR7/Eight-agonist-loaded nanoparticles promote the polarization of tumour-associated macrophages to reinforce most cancers immunotherapy. Nat. Biomed. Eng. 2, 578–588 (2018).


Sharpe, A. H. & Pauken, Ok. E. The varied capabilities of the PD1 inhibitory pathway. Nat. Rev. Immunol. 18, 153–167 (2018).


Burr, M. L. et al. CMTM6 maintains the expression of PD-L1 and regulates anti-tumour immunity. Nature 549, 101–105 (2017).


Zerdes, I., Matikas, A., Bergh, J., Rassidakis, G. Z. & Foukakis, T. Genetic, transcriptional and post-translational regulation of the programmed loss of life protein ligand 1 in most cancers: biology and medical correlations. Oncogene 37, 4639–4661 (2018).


Maj, T. et al. Oxidative stress controls regulatory T cell apoptosis and suppressor exercise and PD-L1-blockade resistance in tumor. Nat. Immunol. 18, 1332–1341 (2017).


Snyder, A. et al. Contribution of systemic and somatic components to medical response and resistance to PD-L1 blockade in urothelial most cancers: an exploratory multi-omic evaluation. PLoS Med. 14, e1002309 (2017).


Takeda, Y. et al. A TLR3-specific adjuvant relieves innate resistance to PD-L1 blockade with out cytokine toxicity in tumor vaccine immunotherapy. Cell Rep. 19, 1874–1887 (2017).


Tang, H. et al. Facilitating T cell infiltration in tumor microenvironment overcomes resistance to PD-L1 blockade. Most cancers Cell 29, 285–296 (2016).


Bellucci, R. et al. Interferon-gamma-induced activation of JAK1 and JAK2 suppresses tumor cell susceptibility to NK cells by way of upregulation of PD-L1 expression. OncoImmunology four, e1008824 (2015).


Wolfle, S. J. et al. PD-L1 expression on tolerogenic APCs is managed by STAT-Three. Eur. J. Immunol. 41, 413–424 (2011).


Casey, S. C. et al. MYC regulates the antitumor immune response by way of CD47 and PD-L1. Science 352, 227–231 (2016).


Bi, X. W. et al. PD-L1 is upregulated by EBV-driven LMP1 by way of NF-κB pathway and correlates with poor prognosis in pure killer/T-cell lymphoma. J. Hematol. Oncol. 9, 109 (2016).


Lim, S. O. et al. Deubiquitination and stabilization of PD-L1 by CSN5. Most cancers Cell 30, 925–939 (2016).


Mognol, G. P. et al. Exhaustion-associated regulatory areas in CD8+ tumor-infiltrating T cells. Proc. Natl Acad. Sci. USA 114, E2776–E2785 (2017).


Wang, Y. et al. Regulation of PD-L1: rising routes for concentrating on tumor immune evasion. Entrance. Pharmacol. 9, 536 (2018).


Zhang, J. et al. Cyclin D-CDK4 kinase destabilizes PD-L1 through cullin Three-SPOP to regulate most cancers immune surveillance. Nature 553, 91–95 (2018).


Li, C. W. et al. Glycosylation and stabilization of programmed loss of life ligand-1 suppresses T-cell exercise. Nat. Commun. 7, 12632 (2016).


Wang, H. et al. PD-L2 expression in colorectal most cancers: impartial prognostic impact and targetability by deglycosylation. OncoImmunology 6, e1327494 (2017).


Li, C. W. et al. Eradication of triple-negative breast most cancers cells by concentrating on glycosylated PD-L1. Most cancers Cell 33, 187–201.e10 (2018).


Chen, G. et al. Exosomal PD-L1 contributes to immunosuppression and is related to anti-PD-1 response. Nature 560, 382–386 (2018).


Wang, H. et al. HIP1R targets PD-L1 to lysosomal degradation to change T cell-mediated cytotoxicity. Nat. Chem. Biol. 15, 42–50 (2019).


Chen, M. et al. Growth and validation of a novel medical fluorescence in situ hybridization assay to detect JAK2 and PD-L1 amplification: a fluorescence in situ hybridization assay for JAK2 and PD-L1 amplification. Mod. Pathol. 30, 1516–1526 (2017).


Taguchi, T. & Misaki, R. Palmitoylation pilots Ras to recycling endosomes. Small GTPases 2, 82–84 (2011).


Runkle, Ok. B. et al. Inhibition of DHHC20-mediated EGFR palmitoylation creates a dependence on EGFR signaling. Mol. Cell 62, 385–396 (2016).


Gao, X. & Hannoush, R. N. Single-cell imaging of Wnt palmitoylation by the acyltransferase porcupine. Nat. Chem. Biol. 10, 61–68 (2014).


Tukachinsky, H., Petrov, Ok., Watanabe, M. & Salic, A. Mechanism of inhibition of the tumor suppressor Patched by Sonic Hedgehog. Proc. Natl Acad. Sci. USA 113, E5866–E5875 (2016).


Ren, J. et al. CSS-Palm an up to date software program for palmitoylation websites prediction. Protein Eng. Des. Sel. 21, 639–644 (2008).


Weng, S. L., Kao, H. J., Huang, C. H. & Lee, T. Y. MDD-Palm: identification of protein S-palmitoylation websites with substrate motifs primarily based on maximal dependence decomposition. PLoS ONE 12, e0179529 (2017).


Thul, P. J. & Lindskog, C. The human protein atlas: a spatial map of the human proteome. Protein Sci. 27, 233–244 (2018).


Garcia-Diaz, A. et al. Interferon receptor signaling pathways regulating PD-L1 and PD-L2 expression. Cell Rep. 19, 1189–1201 (2017).


Riaz, N. et al. Tumor and microenvironment evolution throughout immunotherapy with nivolumab. Cell 171, 934–949 e915 (2017).


Linder, M. E. & Deschenes, R. J. Palmitoylation: policing protein stability and site visitors. Nat. Rev. Mol. Cell Biol. Eight, 74–84 (2007).


Horita, H., Regulation, A., Hong, S. & Middleton, Ok. Figuring out regulatory posttranslational modifications of PD-L1: a deal with monoubiquitinaton. Neoplasia 19, 346–353 (2017).


Stringer, D. Ok. & Piper, R. C. A single ubiquitin is ample for cargo protein entry into MVBs within the absence of ESCRT ubiquitination. J. Cell Biol. 192, 229–242 (2011).


Takahashi, H., Mayers, J. R., Wang, L., Edwardson, J. M. & Audhya, A. Hrs and STAM perform synergistically to bind ubiquitin-modified cargoes in vitro. Biophys. J. 108, 76–84 (2015).


Wang, H. et al. HIP1R targets PD-L1 to lysosomal degradation to change T cell-mediated cytotoxicity. Nat. Chem. Biol. 15, 42–50 (2019).


Bolhassani, A., Jafarzade, B. S. & Mardani, G. In vitro and in vivo supply of therapeutic proteins utilizing cell penetrating peptides. Peptides 87, 50–63 (2017).


Soragni, A. et al. A designed inhibitor of p53 aggregation rescues p53 tumor suppression in ovarian carcinomas. Most cancers Cell 29, 90–103 (2016).


Liang, L. et al. A designed peptide targets two kinds of modifications of p53 with anti-cancer exercise. Cell Chem. Biol. 25, 761–774.e5 (2018).


Tian, X. et al. Organ-specific metastases obtained by culturing colorectal most cancers cells on tissue-specific decellularized scaffolds. Nat. Biomed. Eng. 2, 443–452 (2018).


Fang, C. et al. Identification of palmitoylated transitional endoplasmic reticulum ATPase by proteomic approach and pan antipalmitoylation antibody. J. Proteome Res. 15, 956–962 (2016).


Yousefi-Salakdeh, E., Johansson, J. & Stromberg, R. A way for S- and O-palmitoylation of peptides: synthesis of pulmonary surfactant protein-C fashions. Biochem. J. 343, 557–562 (1999).

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