References
- Agger, K., Cloos, P.A., Christensen, J., Pasini, D., Rose, S., Rappsilber, J., Issaeva, I., Canaani, E., Salcini, A.E., and Helin, K. (2007). UTX and JMJD3 are histone H3K27 demethylases involved in HOX gene regulation and development. Nature 449, 731-734. https://doi.org/10.1038/nature06145
- Agger, K., Cloos, P.A., Rudkjaer, L., Williams, K., Andersen, G., Christensen, J., and Helin, K. (2009). The H3K27me3 demethylase JMJD3 contributes to the activation of the INK4A-ARF locus in response to oncogene- and stress-induced senescence. Genes Dev. 23, 1171-1176. https://doi.org/10.1101/gad.510809
- Barradas, M., Anderton, E., Acosta, J.C., Li, S., Banito, A., Rodriguez-Niedenfuhr, M., Maertens, G., Banck, M., Zhou, M.M., Walsh, M.J., et al. (2009). Histone demethylase JMJD3 contributes to epigenetic control of INK4a/ARF by oncogenic RAS. Genes Dev. 23, 1177-1182. https://doi.org/10.1101/gad.511109
- Bernstein, B.E., Mikkelsen, T.S., Xie, X., Kamal, M., Huebert, D.J., Cuff, J., Fry, B., Meissner, A., Wernig, M., Plath, K., et al. (2006). A bivalent chromatin structure marks key developmental genes in embryonic stem cells. Cell 125, 315-326. https://doi.org/10.1016/j.cell.2006.02.041
- Beyer, S., Kristensen, M.M., Jensen, K.S., Johansen, J.V., and Staller, P. (2008). The histone demethylases JMJD1A and JMJD2B are transcriptional targets of hypoxia-inducible factor HIF. J. Biol. Chem. 283, 36542-36552. https://doi.org/10.1074/jbc.M804578200
- Bruick, R.K., and McKnight, S.L. (2001). A conserved family of prolyl-4-hydroxylases that modify HIF. Science 294, 1337-1340. https://doi.org/10.1126/science.1066373
- Cartharius, K., Frech, K., Grote, K., Klocke, B., Haltmeier, M., Klingenhoff, A., Frisch, M., Bayerlein, M., and Werner, T. (2005). MatInspector and beyond: promoter analysis based on transcription factor binding sites. Bioinformatics 21, 2933-2942. https://doi.org/10.1093/bioinformatics/bti473
- Chen, Z., Zang, J., Whetstine, J., Hong, X., Davrazou, F., Kutateladze, T.G., Simpson, M., Mao, Q., Pan, C.H., Dai, S., et al. (2006). Structural insights into histone demethylation by JMJD2 family members. Cell 125, 691-702. https://doi.org/10.1016/j.cell.2006.04.024
- Choi, S.M., Choi, K.O., Park, Y.K., Cho, H., Yang, E.G., and Park, H. (2006). Clioquinol, a Cu(II)/Zn(II) chelator, inhibits both ubiquitination and asparagine hydroxylation of hypoxia-inducible factor-1alpha, leading to expression of vascular endothelial growth factor and erythropoietin in normoxic cells. J. Biol. Chem. 281, 34056-34063. https://doi.org/10.1074/jbc.M603913200
- Choi, S.M., Oh, H., and Park, H. (2008). Microarray analyses of hypoxia-regulated genes in an aryl hydrocarbon receptor nuclear translocator (Arnt)-dependent manner. FEBS J. 275, 5618-5634. https://doi.org/10.1111/j.1742-4658.2008.06686.x
- De Santa, F., Totaro, M.G., Prosperini, E., Notarbartolo, S., Testa, G., and Natoli, G. (2007). The histone H3 lysine-27 demethylase Jmjd3 links inflammation to inhibition of polycomb-mediated gene silencing. Cell 130, 1083-1094. https://doi.org/10.1016/j.cell.2007.08.019
- Elvidge, G.P., Glenny, L., Appelhoff, R.J., Ratcliffe, P.J., Ragoussis, J., and Gleadle, J.M. (2006). Concordant regulation of gene expression by hypoxia and 2-oxoglutarate-dependent dioxygenase inhibition: the role of HIF-1alpha, HIF-2alpha, and other pathways. J. Biol. Chem. 281, 15215-15226. https://doi.org/10.1074/jbc.M511408200
- Farrall, A.L., and Whitelaw, M.L. (2009). The HIF1alpha-inducible procell death gene BNIP3 is a novel target of SIM2s repression through cross-talk on the hypoxia response element. Oncogene 28, 3671-3680. https://doi.org/10.1038/onc.2009.228
- Gao, X., Wang, Q., Li, W., Yang, B., Song, H., Ju, W., Liu, S., and Cheng, J. (2011). Identification of nucleolar and coiled-body phosphoprotein 1 (NOLC1) minimal promoter regulated by NFkappaB and CREB. BMB Rep. 44, 70-75. https://doi.org/10.5483/BMBRep.2011.44.1.70
- Hewitson, K.S., McNeill, L.A., Riordan, M.V., Tian, Y.M., Bullock, A.N., Welford, R.W., Elkins, J.M., Oldham, N.J., Bhattacharya, S., Gleadle, J.M., et al. (2002). Hypoxia-inducible factor (HIF) asparagine hydroxylase is identical to factor inhibiting HIF (FIH) and is related to the cupin structural family. J. Biol. Chem. 277, 26351-26355. https://doi.org/10.1074/jbc.C200273200
- Hewitson, K.S., Lienard, B.M., McDonough, M.A., Clifton, I.J., Butler, D., Soares, A.S., Oldham, N.J., McNeill, L.A., and Schofield, C.J. (2007). Structural and mechanistic studies on the inhibition of the hypoxia-inducible transcription factor hydroxylases by tricarboxylic acid cycle intermediates. J. Biol. Chem. 282, 3293-3301. https://doi.org/10.1074/jbc.M608337200
- Ko, H.P., Okino, S.T., Ma, Q., and Whitlock, J.P., Jr. (1996). Dioxininduced CYP1A1 transcription in vivo: the aromatic hydrocarbon receptor mediates transactivation, enhancer-promoter communication, and changes in chromatin structure. Mol. Cell. Biol. 16, 430-436. https://doi.org/10.1128/MCB.16.1.430
- Kooistra, S.M., and Helin, K. (2012). Molecular mechanisms and potential functions of histone demethylases. Nat. Rev. Mol. Cell Biol. 13, 297-311. https://doi.org/10.1038/nrm3327
- Kouskouti, A., Scheer, E., Staub, A., Tora, L., and Talianidis, I. (2004). Gene-specific modulation of TAF10 function by SET9-mediated methylation. Mol. Cell. 14, 175-182. https://doi.org/10.1016/S1097-2765(04)00182-0
- Lee, C., Kim, S.J., Jeong, D.G., Lee, S.M., and Ryu, S.E. (2003) Structure of human FIH-1 reveals a unique active site pocket and interaction sites for HIF-1 and von Hippel-Lindau. J. Biol. Chem. 278, 7558-7563. https://doi.org/10.1074/jbc.M210385200
- Maxwell, P.H., Wiesener, M.S., Chang, G.W., Clifford, S.C., Vaux, E.C., Cockman, M.E., Wykoff, C.C., Pugh, C.W., Maher, E.R., and Ratcliffe, P.J. (1999). The tumour suppressor protein VHL targets hypoxia-inducible factors for oxygen-dependent proteolysis. Nature 399, 271-275. https://doi.org/10.1038/20459
- Park, Y.K., and Park, H. (2010). Prevention of CCAAT/enhancerbinding protein beta DNA binding by hypoxia during adipogenesis. J. Biol. Chem. 285, 3289-3299. https://doi.org/10.1074/jbc.M109.059212
- Park, Y.K., and Park, H. (2012). Differentiated embryo chondrocyte 1 (DEC1) represses PPARgamma2 gene through interacting with CCAAT/enhancer binding protein beta (C/EBPbeta). Mol. Cells 33, 575-581. https://doi.org/10.1007/s10059-012-0002-9
- Park, Y.K., Park, B., Lee, S., Choi, K., Moon, Y., and Park, H. (2013). Hypoxia-inducible factor-2alpha-dependent hypoxic induction of Wnt10b expression in adipogenic cells. J. Biol. Chem. 288, 26311-26322. https://doi.org/10.1074/jbc.M113.500835
- Pollard, P.J., Loenarz, C., Mole, D.R., McDonough, M.A., Gleadle, J.M., Schofield, C.J., and Ratcliffe, P.J. (2008). Regulation of Jumonji-domain-containing histone demethylases by hypoxiainducible factor (HIF)-1alpha. Biochem. J. 416, 387-394. https://doi.org/10.1042/BJ20081238
- Schodel, J., Oikonomopoulos, S., Ragoussis, J., Pugh, C.W., Ratcliffe, P.J., and Mole, D.R. (2011). High-resolution genome-wide mapping of HIF-binding sites by ChIP-seq. Blood 117, e207-217. https://doi.org/10.1182/blood-2010-10-314427
- Semenza, G.L. (2012). Hypoxia-inducible factors in physiology and medicine. Cell 148, 399-408. https://doi.org/10.1016/j.cell.2012.01.021
- Shi, Y., and Whetstine, J.R. (2007). Dynamic regulation of histone lysine methylation by demethylases. Mol. Cell 25, 1-14. https://doi.org/10.1016/j.molcel.2006.12.010
- Wellmann, S., Bettkober, M., Zelmer, A., Seeger, K., Faigle, M., Eltzschig, H.K., and Buhrer, C. (2008). Hypoxia upregulates the histone demethylase JMJD1A via HIF-1. Biochem. Biophys. Res. Commun. 372, 892-897. https://doi.org/10.1016/j.bbrc.2008.05.150
- Woon Kim, Y., Kim, S., Geun Kim, C., and Kim, A. (2011). The distinctive roles of erythroid specific activator GATA-1 and NFE2 in transcription of the human fetal gamma-globin genes. Nucleic Acids Res. 39, 6944-6955. https://doi.org/10.1093/nar/gkr253
- Xia, X., and Kung, A.L. (2009). Preferential binding of HIF-1 to transcriptionally active loci determines cell-type specific response to hypoxia. Genome Biol. 10, R113. https://doi.org/10.1186/gb-2009-10-10-r113
- Xia, X., Lemieux, M.E., Li, W., Carroll, J.S., Brown, M., Liu, X.S., and Kung, A.L. (2009). Integrative analysis of HIF binding and transactivation reveals its role in maintaining histone methylation homeostasis. Proc. Natl. Acad. Sci. USA 106, 4260-4265. https://doi.org/10.1073/pnas.0810067106
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