STAMBP promotes lung adenocarcinoma metastasis by regulating the EGFR/MAPK signaling pathway

Neoplasia - Tập 23 - Trang 607-623 - 2021
Hui Xu1,2, Xiaomei Yang2,3, Xiaofeng Xuan2,4, Di Wu2, Jieru Zhang2,4, Xinchun Xu2,5, Yuanjie Zhao2,6, Chunping Ma1, Dawei Li2,7
1Department of Thoracic Surgery, The Affiliated Zhangjiagang Hospital of Soochow University, 68 Jiyang West Road, Suzhou, 215600, China
2Center for Translational Medicine, The Affiliated Zhangjiagang Hospital of Soochow University, 68 Jiyang West Road, Suzhou, 215600, China
3Department of Emergency, The Affiliated Zhangjiagang Hospital of Soochow University, 68 Jiyang West Road, Suzhou, 215600, China
4Department of Respiratory & Critical Care Medicine, The Affiliated Zhangjiagang Hospital of Soochow University, 68 Jiyang West Road, Suzhou, 215600, China
5Department of Ultrasound, The Affiliated Zhangjiagang Hospital of Soochow University, 68 Jiyang West Road, Suzhou, 215600, China
6Department of General Surgery, The Affiliated Zhangjiagang Hospital of Soochow University, 68 Jiyang West Road, Suzhou, 215600, China
7Lead contact

Tài liệu tham khảo

Siegel, 2020, Cancer statistics, 2020, CA Cancer J Clin, 70, 7, 10.3322/caac.21590 Herbst, 2008, Lung cancer, N Engl J Med, 359, 1367, 10.1056/NEJMra0802714 Altorki, 2019, The lung microenvironment: an important regulator of tumour growth and metastasis, Nat Rev Cancer, 19, 9, 10.1038/s41568-018-0081-9 Tomas, 2014, EGF receptor trafficking: consequences for signaling and cancer, Trends Cell Biol, 24, 26, 10.1016/j.tcb.2013.11.002 da Cunha Santos, 2011, EGFR mutations and lung cancer, Annu Rev Pathol, 6, 49, 10.1146/annurev-pathol-011110-130206 Ciardiello, 2008, EGFR antagonists in cancer treatment, N Engl J Med, 358, 1160, 10.1056/NEJMra0707704 Levkowitz, 1998, c-Cbl/Sli-1 regulates endocytic sorting and ubiquitination of the epidermal growth factor receptor, Genes Dev, 12, 3663, 10.1101/gad.12.23.3663 Huang, 2013, Lysine 63-linked polyubiquitination is required for EGF receptor degradation, Proc Natl Acad Sci U S A, 110, 15722, 10.1073/pnas.1308014110 Roberts, 2007, Targeting the Raf-MEK-ERK mitogen-activated protein kinase cascade for the treatment of cancer, Oncogene, 26, 3291, 10.1038/sj.onc.1210422 McCullough, 2004, AMSH is an endosome-associated ubiquitin isopeptidase, J Cell Biol, 166, 487, 10.1083/jcb.200401141 McCullough, 2006, Activation of the endosome-associated ubiquitin isopeptidase AMSH by STAM, a component of the multivesicular body-sorting machinery, Curr Biol, 16, 160, 10.1016/j.cub.2005.11.073 Baiady, 2016, The Vps27/Hrs/STAM (VHS) domain of the Signal-transducing Adaptor Molecule (STAM) directs associated molecule with the SH3 domain of STAM (AMSH) specificity to longer ubiquitin chains and dictates the position of cleavage, J Biol Chem, 291, 2033, 10.1074/jbc.M115.689869 Tanaka, 1999, Possible involvement of a novel STAM-associated molecule "AMSH" in intracellular signal transduction mediated by cytokines, J Biol Chem, 274, 19129, 10.1074/jbc.274.27.19129 Davies, 2013, Mechanism of recruitment and activation of the endosome-associated deubiquitinase AMSH, Biochemistry, 52, 7818, 10.1021/bi401106b Gatta, 2019, The ESCRT-machinery: closing holes and expanding roles, Curr Opin Cell Biol, 59, 121, 10.1016/j.ceb.2019.04.005 Sierra, 2010, AMSH interacts with ESCRT-0 to regulate the stability and trafficking of CXCR4, J Biol Chem, 285, 13990, 10.1074/jbc.M109.061309 Agromayor, 2006, Interaction of AMSH with ESCRT-III and deubiquitination of endosomal cargo, J Biol Chem, 281, 23083, 10.1074/jbc.M513803200 Solomons, 2011, Structural basis for ESCRT-III CHMP3 recruitment of AMSH, Structure, 19, 1149, 10.1016/j.str.2011.05.011 Kyuuma, 2007, AMSH, an ESCRT-III associated enzyme, deubiquitinates cargo on MVB/late endosomes, Cell Struct Funct, 31, 159, 10.1247/csf.06023 Nakamura, 2006, Clathrin anchors deubiquitinating enzymes, AMSH and AMSH-like protein, on early endosomes, Genes Cells, 11, 593, 10.1111/j.1365-2443.2006.00963.x Ishii, 2001, Loss of neurons in the hippocampus and cerebral cortex of AMSH-deficient mice, Mol Cell Biol, 21, 8626, 10.1128/MCB.21.24.8626-8637.2001 McDonell, 2013, Mutations in STAMBP, encoding a deubiquitinating enzyme, cause microcephaly-capillary malformation syndrome, Nat Genet, 45, 556, 10.1038/ng.2602 Faqeih, 2015, Novel STAMBP mutation and additional findings in an Arabic family, Am J Med Genet A, 167A, 805, 10.1002/ajmg.a.36782 Hori, 2018, A novel homozygous missense mutation in the SH3-binding motif of STAMBP causing microcephaly-capillary malformation syndrome, J Hum Genet, 63, 957, 10.1038/s10038-018-0482-3 Wu, 2019, Earlyonset epilepsy and microcephalycapillary malformation syndrome caused by a novel STAMBP mutation in a Chinese boy, Mol Med Rep, 20, 5145 Bednash, 2017, Targeting the deubiquitinase STAMBP inhibits NALP7 inflammasome activity, Nat Commun, 8, 15203, 10.1038/ncomms15203 Hasdemir, 2009, Endosomal deubiquitinating enzymes control ubiquitination and down-regulation of protease-activated receptor 2, J Biol Chem, 284, 28453, 10.1074/jbc.M109.025692 Herrera-Vigenor, 2006, AMSH regulates calcium-sensing receptor signaling through direct interactions, Biochem Biophys Res Commun, 347, 924, 10.1016/j.bbrc.2006.06.169 Ribeiro-Rodrigues, 2014, AMSH-mediated deubiquitination of Cx43 regulates internalization and degradation of gap junctions, FASEB J, 28, 4629, 10.1096/fj.13-248963 Meijer, 2012, Recycling of EGFR and ErbB2 is associated with impaired Hrs tyrosine phosphorylation and decreased deubiquitination by AMSH, Cell Signal, 24, 1981, 10.1016/j.cellsig.2012.07.006 Ma, 2007, Targeting of AMSH to endosomes is required for epidermal growth factor receptor degradation, J Biol Chem, 282, 9805, 10.1074/jbc.M611635200 Iwakami, 2018, STAM-binding protein regulates melanoma metastasis through SLUG stabilization, Biochem Biophys Res Commun, 507, 484, 10.1016/j.bbrc.2018.11.068 Stearman, 2005, Analysis of orthologous gene expression between human pulmonary adenocarcinoma and a carcinogen-induced murine model, Am J Pathol, 167, 1763, 10.1016/S0002-9440(10)61257-6 Cerami, 2012, The cBio cancer genomics portal: an open platform for exploring multidimensional cancer genomics data, Cancer Discov, 2, 401, 10.1158/2159-8290.CD-12-0095 Gao, 2013, Integrative analysis of complex cancer genomics and clinical profiles using the cBioPortal, Sci Signal, 6, pl1, 10.1126/scisignal.2004088 Zhang, 2020, Deubiquitinase UCHL5 is elevated and associated with a poor clinical outcome in lung adenocarcinoma (LUAD), J Cancer, 11, 6675, 10.7150/jca.46146 Li, 2020, OTUD5 cooperates with TRIM25 in transcriptional regulation and tumor progression via deubiquitination activity, Nat Commun, 11, 4184, 10.1038/s41467-020-17926-7 Harrigan, 2018, Deubiquitylating enzymes and drug discovery: emerging opportunities, Nat Rev Drug Discov, 17, 57, 10.1038/nrd.2017.152 Zhang, 2020, Upregulation of deubiquitinase PSMD14 in lung adenocarcinoma (LUAD) and its prognostic significance, J Cancer, 11, 2962, 10.7150/jca.39539 Riihimaki, 2014, Metastatic sites and survival in lung cancer, Lung Cancer, 86, 78, 10.1016/j.lungcan.2014.07.020 Planchard, 2018, Metastatic non-small cell lung cancer: ESMO clinical practice guidelines for diagnosis, treatment and follow-up, Ann Oncol, 29, iv192, 10.1093/annonc/mdy275 Travis, 2011, International association for the study of lung cancer/american thoracic society/european respiratory society international multidisciplinary classification of lung adenocarcinoma, J Thorac Oncol, 6, 244, 10.1097/JTO.0b013e318206a221 Sulahian, 2019, Synthetic lethal interaction of SHOC2 depletion with MEK inhibition in RAS-driven cancers, Cell Rep, 29, 118, 10.1016/j.celrep.2019.08.090 Terai, 2021, SHOC2 is a critical modulator of sensitivity to EGFR-TKIs in non-small cell lung cancer cells, Mol Cancer Res, 19, 317, 10.1158/1541-7786.MCR-20-0664 Lin, 2015, The Hippo effector YAP promotes resistance to RAF- and MEK-targeted cancer therapies, Nat Genet, 47, 250, 10.1038/ng.3218 Kurppa, 2020, Treatment-induced tumor dormancy through YAP-mediated transcriptional reprogramming of the apoptotic pathway, Cancer Cell, 37, 104, 10.1016/j.ccell.2019.12.006 Pao, 2010, Rational, biologically based treatment of EGFR-mutant non-small-cell lung cancer, Nat Rev Cancer, 10, 760, 10.1038/nrc2947 Gelsomino, 2013, Epidermal growth factor receptor tyrosine kinase inhibitor treatment in patients with EGFR wild-type non-small-cell lung cancer: the never-ending story, J Clin Oncol, 31, 3291, 10.1200/JCO.2013.50.2617 Menard, 2018, Reactivation of mutant-EGFR degradation through clathrin inhibition overcomes resistance to EGFR tyrosine kinase inhibitors, Cancer Res, 78, 3267, 10.1158/0008-5472.CAN-17-2195 Dykxhoorn, 2006, The silent treatment: siRNAs as small molecule drugs, Gene Ther, 13, 541, 10.1038/sj.gt.3302703 Tam, 2013, Advances in lipid nanoparticles for siRNA delivery, Pharmaceutics, 5, 498, 10.3390/pharmaceutics5030498 Cheng, 2020, Discovery of potent and selective Epidermal Growth Factor Receptor (EGFR) bifunctional small-molecule degraders, J Med Chem, 63, 1216, 10.1021/acs.jmedchem.9b01566 Leung, 2016, Targeting tyrosine kinase inhibitor-resistant non-small cell lung cancer by inducing epidermal growth factor receptor degradation via methionine 790 oxidation, Antioxid Redox Signal, 24, 263, 10.1089/ars.2015.6420 Yao, 2020, Discovery of a novel EGFR ligand DPBA that degrades EGFR and suppresses EGFR-positive NSCLC growth, Signal Transduct Target Ther, 5, 214, 10.1038/s41392-020-00251-2 Conte, 2016, Chapter six - The ubiquitin network in the control of EGFR endocytosis and signaling, Prog Mol Biol Transl Sci, 141, 225, 10.1016/bs.pmbts.2016.03.002 Huang, 2006, Differential regulation of EGF receptor internalization and degradation by multiubiquitination within the kinase domain, Mol Cell, 21, 737, 10.1016/j.molcel.2006.02.018 Eden, 2012, The role of EGF receptor ubiquitination in regulating its intracellular traffic, Traffic, 13, 329, 10.1111/j.1600-0854.2011.01305.x