MARS2 drives metabolic switch of non-small-cell lung cancer cells via interaction with MCU
Tài liệu tham khảo
Park, 2008, Aminoacyl tRNA synthetases and their connections to disease, Proc. Natl. Acad. Sci. U.S.A., 105, 11043, 10.1073/pnas.0802862105
Gomez, 2020, Aminoacyl-tRNA synthetases, Cold Spring Harbor Laboratory Press for the RNA Society, 26, 910
Konovalova, 2013, Mitochondrial aminoacyl-tRNA synthetases in human disease, Mol. Genet. Metabol., 108, 206, 10.1016/j.ymgme.2013.01.010
Kwon, 2011, Dual role of methionyl-tRNA synthetase in the regulation of translation and tumor suppressor activity of aminoacyl-tRNA synthetase-interacting multifunctional protein-3, Proc. Natl. Acad. Sci. U. S. A., 108, 19635, 10.1073/pnas.1103922108
Spencer, 2004, Characterization of the human mitochondrial methionyl-tRNA synthetase, Biochemistry, 43, 9743, 10.1021/bi049639w
Rizzuto, 2012, Mitochondria as sensors and regulators of calcium signalling, Nat. Rev. Mol. Cell Biol., 13, 566, 10.1038/nrm3412
Romero-Garcia, 2019, Mitochondrial calcium: transport and modulation of cellular processes in homeostasis and cancer, Int. J. Oncol., 54, 1155
De Stefani, 2015, Structure and function of the mitochondrial calcium uniporter complex, Biochim. Biophys. Acta Mol. Cell Res., 1853, 2006, 10.1016/j.bbamcr.2015.04.008
Vyas, 2016, Mitochondria and cancer, Cell, 166, 555, 10.1016/j.cell.2016.07.002
Bensaad, 2006, TIGAR, a p53-inducible regulator of glycolysis and apoptosis, Cell, 126, 107, 10.1016/j.cell.2006.05.036
Warburg, 1956, On the origin of cancer cells, Science, 123, 309, 10.1126/science.123.3191.309
Maddocks, 2011, Metabolic regulation by p53, J. Mol. Med. (Berl.), 89, 237, 10.1007/s00109-011-0735-5
Giorgi, 2012, Mitochondrial Ca2+ and apoptosis, Cell Calcium, 52, 36, 10.1016/j.ceca.2012.02.008
Pozzan, 2009, Measurements of mitochondrial calcium in vivo, Biochim. Biophys. Acta, 1787, 1317, 10.1016/j.bbabio.2008.11.012
Pan, 2013, The physiological role of mitochondrial calcium revealed by mice lacking the mitochondrial calcium uniporter, Nat. Cell Biol., 15, 1464, 10.1038/ncb2868
De Stefani, 2011, A forty-kilodalton protein of the inner membrane is the mitochondrial calcium uniporter, Nature, 476, 336, 10.1038/nature10230
Onesti, 2000, Structural studies of lysyl-tRNA synthetase: conformational changes induced by substrate binding, Biochemistry, 39, 12853, 10.1021/bi001487r
Serre, 2001, How methionyl-tRNA synthetase creates its amino acid recognition pocket upon L-methionine binding, J. Mol. Biol., 306, 863, 10.1006/jmbi.2001.4408
Crepin, 2003, Use of analogues of methionine and methionyl adenylate to sample conformational changes during catalysis in Escherichia coli methionyl-tRNA synthetase, J. Mol. Biol., 332, 59, 10.1016/S0022-2836(03)00917-3
Rosevear, 1988, Purification and NMR studies of [methyl-13C]methionine-labeled truncated methionyl-tRNA synthetase, Biochemistry, 27, 7931, 10.1021/bi00420a052
Couchonnal, 2008, The role of calmodulin kinase II in myocardial physiology and disease, Physiology, 23, 151, 10.1152/physiol.00043.2007
Hook, 2001, Ca2+/CaM-dependent kinases: from activation to function, Annu. Rev. Pharmacol. Toxicol., 41, 471, 10.1146/annurev.pharmtox.41.1.471
Sheng, 1991, CREB: a Ca(2+)-regulated transcription factor phosphorylated by calmodulin-dependent kinases, Science, 252, 1427, 10.1126/science.1646483
Sun, 1994, Differential activation of CREB by Ca2+/calmodulin-dependent protein kinases type II and type IV involves phosphorylation of a site that negatively regulates activity, Genes Dev., 8, 2527, 10.1101/gad.8.21.2527
Okoshi, 2009, Transcriptional regulation of tumor suppressor p53 by cAMP-responsive element-binding protein/AMP-activated protein kinase complex in response to glucose deprivation, Gene Cell., 14, 1429, 10.1111/j.1365-2443.2009.01359.x
Guerra, 2017, Mitochondrial dysfunction: a novel potential driver of epithelial-to-mesenchymal transition in cancer, Front. Oncol., 7, 295, 10.3389/fonc.2017.00295
Polyak, 2009, Transitions between epithelial and mesenchymal states: acquisition of malignant and stem cell traits, Nat. Rev. Cancer, 9, 265, 10.1038/nrc2620
Cheng, 2011, Inhibition of p53 represses E-cadherin expression by increasing DNA methyltransferase-1 and promoter methylation in serous borderline ovarian tumor cells, Oncogene, 30, 3930, 10.1038/onc.2011.117
Lim, 2008, Epigenetic changes induced by reactive oxygen species in hepatocellular carcinoma: methylation of the E-cadherin promoter, Gastroenterology, 135, 2128, 10.1053/j.gastro.2008.07.027
Winkler, 2020, Concepts of extracellular matrix remodelling in tumour progression and metastasis, Nat. Commun., 11, 5120, 10.1038/s41467-020-18794-x
Hung, 2010, Skp2 overexpression increases the expression of MMP-2 and MMP-9 and invasion of lung cancer cells, Cancer Lett., 288, 156, 10.1016/j.canlet.2009.06.032
Dufour, 2008, Role of the hemopexin domain of matrix metalloproteinases in cell migration, J. Cell. Physiol., 217, 643, 10.1002/jcp.21535
Gregory, 2008, The miR-200 family and miR-205 regulate epithelial to mesenchymal transition by targeting ZEB1 and SIP1, Nat. Cell Biol., 10, 593, 10.1038/ncb1722
Xu, 2009, TGF-beta-induced epithelial to mesenchymal transition, Cell Res., 19, 156, 10.1038/cr.2009.5
Larsen, 2016, ZEB1 drives epithelial-to-mesenchymal transition in lung cancer, J. Clin. Invest., 126, 3219, 10.1172/JCI76725
Wu, 2012, Canonical Wnt signaling regulates Slug activity and links epithelial-mesenchymal transition with epigenetic Breast Cancer 1, Early Onset (BRCA1) repression, Proc. Natl. Acad. Sci. U.S.A., 109, 16654, 10.1073/pnas.1205822109
Wang, 2014, ASPP2 controls epithelial plasticity and inhibits metastasis through beta-catenin-dependent regulation of ZEB1, Nat. Cell Biol., 16, 1092, 10.1038/ncb3050
Tenbaum, 2012, beta-catenin confers resistance to PI3K and AKT inhibitors and subverts FOXO3a to promote metastasis in colon cancer, Nat. Med., 18, 892, 10.1038/nm.2772
Yang, 2017, FOXP3 promotes tumor growth and metastasis by activating Wnt/beta-catenin signaling pathway and EMT in non-small cell lung cancer, Mol. Cancer, 16, 124, 10.1186/s12943-017-0700-1
Travis, 2002, Pathology of lung cancer, Clin. Chest Med., 23, 65, 10.1016/S0272-5231(03)00061-3
Bareschino, 2011, Treatment of advanced non small cell lung cancer, J. Thorac. Dis., 3, 122
Wallace, 2012, Mitochondria and cancer, Nat. Rev. Cancer, 12, 685, 10.1038/nrc3365
Patron, 2014, MICU1 and MICU2 finely tune the mitochondrial Ca2+ uniporter by exerting opposite effects on MCU activity, Mol. Cell, 53, 726, 10.1016/j.molcel.2014.01.013
Tomar, 2016, MCUR1 is a scaffold factor for the MCU complex function and promotes mitochondrial bioenergetics, Cell Rep., 15, 1673, 10.1016/j.celrep.2016.04.050
Joiner, 2012, CaMKII determines mitochondrial stress responses in heart, Nature, 491, 269, 10.1038/nature11444
Sebag, 2017, Mitochondrial CaMKII inhibition in airway epithelium protects against allergic asthma, JCI Insight, 2, 10.1172/jci.insight.88297
Yoast, 2021, The Mitochondrial Ca(2+) uniporter is a central regulator of interorganellar Ca(2+) transfer and NFAT activation, J. Biol. Chem., 297, 10.1016/j.jbc.2021.101174
Koval, 2019, Loss of MCU prevents mitochondrial fusion in G(1)-S phase and blocks cell cycle progression and proliferation, Sci. Signal., 12, 10.1126/scisignal.aav1439
Jiang, 2011, p53 regulates biosynthesis through direct inactivation of glucose-6-phosphate dehydrogenase, Nat. Cell Biol., 13, 310, 10.1038/ncb2172
Stanton, 2012, Glucose-6-phosphate dehydrogenase, NADPH, and cell survival, IUBMB Life, 64, 362, 10.1002/iub.1017
Kim, 2011, p53 and MicroRNA-34 are suppressors of canonical Wnt signaling, Sci. Signal., 4, 10.1126/scisignal.2001744
Giampazolias, 2016, Mitochondria and the hallmarks of cancer, FEBS J., 283, 803, 10.1111/febs.13603
Tran, 2018, S6 kinase 1 plays a key role in mitochondrial morphology and cellular energy flow, Cell. Signal., 48, 13, 10.1016/j.cellsig.2018.04.002
Kweon, 2004, Golgi enzymes are enriched in perforated zones of golgi cisternae but are depleted in COPI vesicles, Mol. Biol. Cell, 15, 4710, 10.1091/mbc.e03-12-0881
Tokuyasu, 1980, Immunochemistry on ultrathin frozen sections, Histochem. J., 12, 381, 10.1007/BF01011956