Post-translational regulations of PD-L1 and PD-1: Mechanisms and opportunities for combined immunotherapy
Tài liệu tham khảo
Pardoll, 2012, The blockade of immune checkpoints in cancer immunotherapy, Nat. Rev. Cancer, 12, 252, 10.1038/nrc3239
Sharma, 2015, The future of immune checkpoint therapy, Science, 348, 56, 10.1126/science.aaa8172
Iwai, 2017, Cancer immunotherapies targeting the PD-1 signaling pathway, J. Biomed. Sci., 24, 26, 10.1186/s12929-017-0329-9
Hargadon, 2018, Immune checkpoint blockade therapy for cancer: an overview of FDA-approved immune checkpoint inhibitors, Int. Immunopharmacol., 62, 29, 10.1016/j.intimp.2018.06.001
Ishida, 1992, Induced expression of PD-1, a novel member of the immunoglobulin gene superfamily, upon programmed cell death, EMBO J., 11, 3887, 10.1002/j.1460-2075.1992.tb05481.x
Agata, 1996, Expression of the PD-1 antigen on the surface of stimulated mouse T and B lymphocytes, Int. Immunol., 8, 765, 10.1093/intimm/8.5.765
Keir, 2008, PD-1 and its ligands in tolerance and immunity, Annu. Rev. Immunol., 26, 677, 10.1146/annurev.immunol.26.021607.090331
Sharpe, 2018, The diverse functions of the PD1 inhibitory pathway, Nat. Rev. Immunol., 18, 153, 10.1038/nri.2017.108
Schildberg, 2016, Coinhibitory pathways in the B7-CD28 ligand-receptor family, Immunity, 44, 955, 10.1016/j.immuni.2016.05.002
Pitt, 2016, Resistance mechanisms to immune-checkpoint blockade in cancer: tumor-Intrinsic and -extrinsic factors, Immunity, 44, 1255, 10.1016/j.immuni.2016.06.001
Yarchoan, 2017, Tumor mutational burden and response rate to PD-1 inhibition, N. Engl. J. Med., 377, 2500, 10.1056/NEJMc1713444
Bally, 2016, Genetic and epigenetic regulation of PD-1 expression, J. Immunol., 196, 2431, 10.4049/jimmunol.1502643
Chen, 2016, Regulation of PD-L1: a novel role of pro-survival signalling in cancer, Ann. Oncol., 27, 409, 10.1093/annonc/mdv615
Sun, 2018, Regulation and function of the PD-L1 checkpoint, Immunity, 48, 434, 10.1016/j.immuni.2018.03.014
Liu, 2016, Post-translational modification control of innate immunity, Immunity, 45, 15, 10.1016/j.immuni.2016.06.020
Rape, 2018, Ubiquitylation at the crossroads of development and disease, Nat. Rev. Mol. Cell Biol., 19, 59, 10.1038/nrm.2017.83
Wang, 2020, RBR E3 ubiquitin ligases in tumorigenesis, Semin. Cancer Biol., 10.1016/j.semcancer.2020.05.002
Li, 2016, Glycosylation and stabilization of programmed death ligand-1 suppresses T-cell activity, Nat. Commun., 7, 12632, 10.1038/ncomms12632
Deng, 2019, Inhibition of mTOR complex 1/p70 S6 kinase signaling elevates PD-L1 levels in human cancer cells through enhancing protein stabilization accompanied with enhanced beta-TrCP degradation, Oncogene, 38, 6270, 10.1038/s41388-019-0877-4
Zhang, 2018, Cyclin D-CDK4 kinase destabilizes PD-L1 via cullin 3-SPOP to control cancer immune surveillance, Nature, 553, 91, 10.1038/nature25015
Cha, 2018, Metformin promotes antitumor immunity via endoplasmic-reticulum-Associated degradation of PD-L1, Mol. Cell, 71, 606, 10.1016/j.molcel.2018.07.030
Burr, 2017, CMTM6 maintains the expression of PD-L1 and regulates anti-tumour immunity, Nature, 549, 101, 10.1038/nature23643
Mezzadra, 2017, Identification of CMTM6 and CMTM4 as PD-L1 protein regulators, Nature, 549, 106, 10.1038/nature23669
Sakamoto, 2001, Protacs: chimeric molecules that target proteins to the Skp1-Cullin-F box complex for ubiquitination and degradation, Proc. Natl. Acad. Sci. U. S. A., 98, 8554, 10.1073/pnas.141230798
Liu, 2020, PROTACs: a novel strategy for cancer therapy, Semin. Cancer Biol., 67, 171, 10.1016/j.semcancer.2020.02.006
Pettersson, 2019, PROteolysis TArgeting Chimeras (PROTACs) - past, present and future, Drug Discov. Today Technol., 31, 15, 10.1016/j.ddtec.2019.01.002
Cheng, 2020, Discovery of novel resorcinol diphenyl ether-based PROTAC-like molecules as dual inhibitors and degraders of PD-L1, Eur. J. Med. Chem., 199, 10.1016/j.ejmech.2020.112377
Cotton, 2021, Development of antibody-based PROTACs for the degradation of the cell-surface immune checkpoint protein PD-L1, J. Am. Chem. Soc., 143, 593, 10.1021/jacs.0c10008
Banik, 2020, Lysosome-targeting chimaeras for degradation of extracellular proteins, Nature, 584, 291, 10.1038/s41586-020-2545-9
Uhle, 2003, Protein kinase CK2 and protein kinase D are associated with the COP9 signalosome, EMBO J., 22, 1302, 10.1093/emboj/cdg127
Lim, 2016, Deubiquitination and stabilization of PD-L1 by CSN5, Cancer Cell, 30, 925, 10.1016/j.ccell.2016.10.010
Huang, 2019, USP22 deubiquitinates CD274 to suppress anticancer immunity, Cancer Immunol. Res., 7, 1580, 10.1158/2326-6066.CIR-18-0910
Wang, 2020, The deubiquitinase USP22 regulates PD-L1 degradation in human cancer cells, Cell Commun. Signal, 18, 112, 10.1186/s12964-020-00612-y
Jingjing, 2018, Deubiquitination and stabilization of programmed cell death ligand 1 by ubiquitin-specific peptidase 9, X-linked in oral squamous cell carcinoma, Cancer Med., 7, 4004, 10.1002/cam4.1675
Zhu, 2020, Deubiquitinating enzyme OTUB1 promotes cancer cell immunosuppression via preventing ER-associated degradation of immune checkpoint protein PD-L1, Cell Death Differ.
Schauer, 2020, Advances in discovering deubiquitinating enzyme (DUB) inhibitors, J. Med. Chem., 63, 2731, 10.1021/acs.jmedchem.9b01138
Schwarz, 2011, Mechanisms and principles of N-linked protein glycosylation, Curr. Opin. Struct. Biol., 21, 576, 10.1016/j.sbi.2011.08.005
Pinho, 2015, Glycosylation in cancer: mechanisms and clinical implications, Nat. Rev. Cancer, 15, 540, 10.1038/nrc3982
Li, 2018, Eradication of triple-negative breast cancer cells by targeting glycosylated PD-L1, Cancer Cell, 33, 187, 10.1016/j.ccell.2018.01.009
Hsu, 2018, STT3-dependent PD-L1 accumulation on cancer stem cells promotes immune evasion, Nat. Commun., 9, 1908, 10.1038/s41467-018-04313-6
D'Arrigo, 2017, A regulatory role for the co-chaperone FKBP51s in PD-L1 expression in glioma, Oncotarget, 8, 68291, 10.18632/oncotarget.19309
Maher, 2018, Small-molecule Sigma1 modulator induces autophagic degradation of PD-L1, Mol. Cancer Res., 16, 243, 10.1158/1541-7786.MCR-17-0166
Gaali, 2015, Selective inhibitors of the FK506-binding protein 51 by induced fit, Nat. Chem. Biol., 11, 33, 10.1038/nchembio.1699
Cohen, 2002, The origins of protein phosphorylation, Nat. Cell Biol., 4, E127, 10.1038/ncb0502-e127
Li, 2019, MET inhibitors promote liver tumor evasion of the immune response by stabilizing PDL1, Gastroenterology, 156, 1849, 10.1053/j.gastro.2019.01.252
Chan, 2019, IL-6/JAK1 pathway drives PD-L1 Y112 phosphorylation to promote cancer immune evasion, J. Clin. Invest., 129, 3324, 10.1172/JCI126022
Narita, 2019, Functions and mechanisms of non-histone protein acetylation, Nat. Rev. Mol. Cell Biol., 20, 156, 10.1038/s41580-018-0081-3
Horita, 2017, Identifying regulatory posttranslational modifications of PD-L1: a focus on monoubiquitinaton, Neoplasia, 19, 346, 10.1016/j.neo.2017.02.006
Gao, 2020, Acetylation-dependent regulation of PD-L1 nuclear translocation dictates the efficacy of anti-PD-1 immunotherapy, Nat. Cell Biol., 22, 1064, 10.1038/s41556-020-0562-4
Du, 2020, KPNB1-mediated nuclear translocation of PD-L1 promotes non-small cell lung cancer cell proliferation via the Gas6/MerTK signaling pathway, Cell Death Differ.
Hou, 2020, PD-L1-mediated gasdermin C expression switches apoptosis to pyroptosis in cancer cells and facilitates tumour necrosis, Nat. Cell Biol., 22, 1264, 10.1038/s41556-020-0575-z
Yu, 2020, Regulation of sister chromatid cohesion by nuclear PD-L1, Cell Res., 30, 590, 10.1038/s41422-020-0315-8
Walk, 2020, The cancer immunotherapy biomarker testing landscape, Arch. Pathol. Lab. Med., 144, 706, 10.5858/arpa.2018-0584-CP
Resh, 2017, Palmitoylation of proteins in cancer, Biochem. Soc. Trans., 45, 409, 10.1042/BST20160233
De, 2018, Emerging roles of DHHC-mediated protein S-palmitoylation in physiological and pathophysiological context, Eur. J. Cell Biol., 97, 319, 10.1016/j.ejcb.2018.03.005
Yang, 2018, Palmitoylation stabilizes PD-L1 to promote breast tumor growth, Cell Res.
Yao, 2019, Inhibiting PD-L1 palmitoylation enhances T-cell immune responses against tumours, Nat. Biomed. Eng.
Shahid, 2020, S-palmitoylation as a functional regulator of proteins associated with cisplatin resistance in bladder cancer, Int. J. Biol. Sci., 16, 2490, 10.7150/ijbs.45640
Kalluri, 2016, The biology and function of exosomes in cancer, J. Clin. Invest., 126, 1208, 10.1172/JCI81135
Tkach, 2016, Communication by extracellular vesicles: where we are and where we need to go, Cell, 164, 1226, 10.1016/j.cell.2016.01.043
Moreno-Gonzalo, 2014, Post-translational modifications of exosomal proteins, Front. Immunol., 5, 383, 10.3389/fimmu.2014.00383
Smith, 2015, Ubiquitination as a mechanism to transport soluble mycobacterial and eukaryotic proteins to exosomes, J. Immunol., 195, 2722, 10.4049/jimmunol.1403186
Li, 2016, Acetylation modification regulates GRP78 secretion in colon cancer cells, Sci. Rep., 6, 30406, 10.1038/srep30406
Romancino, 2018, Palmitoylation is a post-translational modification of Alix regulating the membrane organization of exosome-like small extracellular vesicles, Biochim. Biophys. Acta Gen. Sub., 1862, 2879, 10.1016/j.bbagen.2018.09.004
Chen, 2018, Exosomal PD-L1 contributes to immunosuppression and is associated with anti-PD-1 response, Nature, 560, 382, 10.1038/s41586-018-0392-8
Yang, 2018, Exosomal PD-L1 harbors active defense function to suppress T cell killing of breast cancer cells and promote tumor growth, Cell Res., 28, 862, 10.1038/s41422-018-0060-4
Poggio, 2019, Suppression of exosomal PD-L1 induces systemic anti-tumor immunity and memory, Cell, 177, 414, 10.1016/j.cell.2019.02.016
Zhou, 2020, Exosomal PD-L1: new insights into tumor immune escape mechanisms and therapeutic strategies, Front. Cell Dev. Biol., 8, 10.3389/fcell.2020.569219
Kim, 2019, Exosomal PD-L1 promotes tumor growth through immune escape in non-small cell lung cancer, Exp. Mol. Med., 51, 1
Liu, 2018, Sensitive detection of exosomal proteins via a compact surface plasmon resonance biosensor for Cancer diagnosis, ACS Sens., 3, 1471, 10.1021/acssensors.8b00230
Li, 2019, Clinical significance of PD-L1 expression in serum-derived exosomes in NSCLC patients, J. Transl. Med., 17, 355, 10.1186/s12967-019-2101-2
Huang, 2020, Homogeneous, low-volume, efficient, and sensitive quantitation of circulating exosomal PD-L1 for cancer diagnosis and immunotherapy response prediction, Angew. Chem. Int. Ed. Engl., 59, 4800, 10.1002/anie.201916039
Yu, 2020, Regulation of PD-1 in T cells for cancer immunotherapy, Eur. J. Pharmacol., 881, 10.1016/j.ejphar.2020.173240
Okada, 2017, Blockage of core fucosylation reduces cell-surface expression of PD-1 and promotes anti-tumor immune responses of t cells, Cell Rep., 20, 1017, 10.1016/j.celrep.2017.07.027
Meng, 2018, FBXO38 mediates PD-1 ubiquitination and regulates anti-tumour immunity of T cells, Nature, 564, 130, 10.1038/s41586-018-0756-0
Zhou, 2020, KLHL22 maintains PD-1 homeostasis and prevents excessive T cell suppression, Proc. Natl. Acad. Sci. U. S. A., 117, 28239, 10.1073/pnas.2004570117
Lyle, 2019, c-Cbl targets PD-1 in immune cells for proteasomal degradation and modulates colorectal tumor growth, Sci. Rep., 9, 20257, 10.1038/s41598-019-56208-1
Liu, 2020, N-glycosylation of PD-1 promotes binding of camrelizumab, EMBO Rep., 10.15252/embr.202051444
Zhang, 2020, Loss of core fucosylation enhances the anticancer activity of cytotoxic T lymphocytes by increasing PD-1 degradation, Eur. J. Immunol., 50, 1820, 10.1002/eji.202048543
Tan, 2017, An unexpected N-terminal loop in PD-1 dominates binding by nivolumab, Nat. Commun., 8, 14369, 10.1038/ncomms14369
Markham, 2019, Camrelizumab: first global approval, Drugs, 79, 1355, 10.1007/s40265-019-01167-0
Jia, 2018, The function of fucosylation in progression of lung cancer, Front. Oncol., 8, 565, 10.3389/fonc.2018.00565
Keeley, 2019, The diverse contributions of fucose linkages in cancer, Cancers (Basel), 11, 10.3390/cancers11091241