Dynamic chromatin regulation at Notch target genes

References

• Hamaguchi Y, Matsunami N, Yamamoto Y, Honjo T. Purification and characterization of a protein that binds to the recombination signal sequence of the immunoglobulin J kappa segment. Nucleic Acids Res 1989; 17:9015-9026; PMID:2511556; http://dx.doi.org/10.1093/nar/17.22.9015
   PubMed Web of Science ®Google Scholar
• Furukawa T, Maruyama S, Kawaichi M, Honjo T. The Drosophila homolog of the immunoglobulin recombination signal-binding protein regulates peripheral nervous system development. Cell 1992; 69:1191-1197; PMID:1617729; http://dx.doi.org/10.1016/0092-8674(92)90640-X
   PubMed Web of Science ®Google Scholar
• Tun T, Hamaguchi Y, Matsunami N, Furukawa T, Honjo T, Kawaichi M. Recognition sequence of a highly conserved DNA binding protein RBP-J kappa. Nucleic Acids Res 1994; 22:965-971; PMID:8152928; http://dx.doi.org/10.1093/nar/22.6.965
   PubMed Web of Science ®Google Scholar
• Borggrefe T, Oswald F. The Notch signaling pathway: transcriptional regulation at Notch target genes. Cell Mol Life Sci 2009; 66:1631-1646; PMID:19165418; http://dx.doi.org/10.1007/s00018-009-8668-7
   PubMed Web of Science ®Google Scholar
• Hein K, Mittler G, Cizelsky W, Kühl M, Ferrante F, Liefke R, Berger IM, Just S, Sträng JE, Kestler HA et al. Site-specific methylation of Notch1 controls the amplitude and duration of the Notch1 response. Sci Signal 2015; 8:ra30; PMID:25805888; http://dx.doi.org/10.1126/scisignal.2005892
   PubMed Web of Science ®Google Scholar
• Borggrefe T, Lauth M, Zwijsen A, Huylebroeck D, Oswald F, Giaimo BD. The Notch intracellular domain integrates signals from Wnt, Hedgehog, TGFbeta/BMP and hypoxia pathways. Biochim Biophys Acta 2016; 1863:303-313; PMID: 26592459; http://dx.doi.org/10.1016/j.bbamcr.2015.11.020
   PubMed Web of Science ®Google Scholar
• Nam Y, Weng AP, Aster JC, Blacklow SC. Structural requirements for assembly of the CSL.intracellular Notch1.Mastermind-like 1 transcriptional activation complex. J Biol Chem 2003; 278:21232-21239; PMID:12644465; http://dx.doi.org/10.1074/jbc.M301567200
   PubMed Web of Science ®Google Scholar
• Kovall RA, Hendrickson WA. Crystal structure of the nuclear effector of Notch signaling, CSL, bound to DNA. EMBO J 2004; 23:3441-3451; PMID:15297877; http://dx.doi.org/10.1038/sj.emboj.7600349
   PubMed Web of Science ®Google Scholar
• Nam Y, Sliz P, Song L, Aster JC, Blacklow SC. Structural basis for cooperativity in recruitment of MAML coactivators to Notch transcription complexes. Cell 2006; 124:973-983; PMID:16530044; http://dx.doi.org/10.1016/j.cell.2005.12.037
   PubMed Web of Science ®Google Scholar
• Wilson JJ, Kovall RA. Crystal structure of the CSL-Notch-Mastermind ternary complex bound to DNA. Cell 2006; 124:985-996; PMID:16530045; http://dx.doi.org/10.1016/j.cell.2006.01.035
   PubMed Web of Science ®Google Scholar
• Geimer Le Lay AS, Oravecz A, Mastio J, Jung C, Marchal P, Ebel C, Dembélé D, Jost B, Le Gras S, Thibault C et al. The tumor suppressor Ikaros shapes the repertoire of notch target genes in T cells. Sci Signal 2014; 7:ra28; PMID:24643801; http://dx.doi.org/10.1126/scisignal.2004545
   PubMed Web of Science ®Google Scholar
• Chari S, Winandy S. Ikaros regulates Notch target gene expression in developing thymocytes. J Immunol 2008; 181:6265-6274; PMID:18941217; http://dx.doi.org/10.4049/jimmunol.181.9.6265
   PubMed Web of Science ®Google Scholar
• Nam Y, Sliz P, Pear WS, Aster JC, Blacklow SC. Cooperative assembly of higher-order Notch complexes functions as a switch to induce transcription. Proc Natl Acad Sci U S A 2007; 104:2103-2108; PMID:17284587; http://dx.doi.org/10.1073/pnas.0611092104
   PubMed Web of Science ®Google Scholar
• Hass MR, Liow HH, Chen X, Sharma A, Inoue YU, Inoue T, Reeb A, Martens A, Fulbright M, Raju S et al. SpDamID: Marking DNA Bound by Protein Complexes Identifies Notch-Dimer Responsive Enhancers. Mol Cell 2015; 59:685-697; PMID:26257285; http://dx.doi.org/10.1016/j.molcel.2015.07.008
   PubMed Web of Science ®Google Scholar
• Liu H, Chi AW, Arnett KL, Chiang MY, Xu L, Shestova O, Wang H, Li YM, Bhandoola A, Aster JC et al. Notch dimerization is required for leukemogenesis and T-cell development. Genes Dev 2010; 24:2395-2407; PMID:20935071; http://dx.doi.org/10.1101/gad.1975210
   PubMed Web of Science ®Google Scholar
• Oswald F, Täuber B, Dobner T, Bourteele S, Kostezka U, Adler G, Liptay S, Schmid RM. p300 acts as a transcriptional coactivator for mammalian Notch-1. Mol Cell Biol 2001; 21:7761-7774; PMID:11604511; http://dx.doi.org/10.1128/MCB.21.22.7761-7774.2001
   PubMed Web of Science ®Google Scholar
• Oswald F, Kostezka U, Astrahantseff K, Bourteele S, Dillinger K, Zechner U, Ludwig L, Wilda M, Hameister H, Knöchel W et al. SHARP is a novel component of the Notch/RBP-Jkappa signaling pathway. EMBO J 2002; 21:5417-5426; PMID:12374742; http://dx.doi.org/10.1093/emboj/cdf549
   PubMed Web of Science ®Google Scholar
• Oswald F, Winkler M, Cao Y, Astrahantseff K, Bourteele S, Knöchel W, Borggrefe T. RBP-Jkappa/SHARP recruits CtIP/CtBP corepressors to silence Notch target genes. Mol Cell Biol 2005; 25:10379-10390; PMID:16287852; http://dx.doi.org/10.1128/MCB.25.23.10379-10390.2005
   PubMed Web of Science ®Google Scholar
• Salat D, Liefke R, Wiedenmann J, Borggrefe T, Oswald F. ETO, but not leukemogenic fusion protein AML1/ETO, augments RBP-Jkappa/SHARP-mediated repression of notch target genes. Mol Cell Biol 2008; 28:3502-3512; PMID:18332109; http://dx.doi.org/10.1128/MCB.01966-07
   PubMed Web of Science ®Google Scholar
• Shi Y, Downes M, Xie W, Kao HY, Ordentlich P, Tsai CC, Hon M, Evans RM. Sharp, an inducible cofactor that integrates nuclear receptor repression and activation. Genes Dev 2001; 15:1140-1151; PMID:11331609; http://dx.doi.org/10.1101/gad.871201
   PubMed Web of Science ®Google Scholar
• Kao HY, Ordentlich P, Koyano-Nakagawa N, Tang Z, Downes M, Kintner CR, Evans RM, Kadesch T. A histone deacetylase corepressor complex regulates the Notch signal transduction pathway. Genes Dev 1998; 12:2269-2277; PMID:9694793; http://dx.doi.org/10.1101/gad.12.15.2269
   PubMed Web of Science ®Google Scholar
• Oswald F, Rodriguez P, Giaimo BD, Antonello ZA, Mira L, Mittler G, Thiel VN, Collins KJ, Tabaja N, Cizelsky W et al. A phospho-dependent mechanism involving NCoR and KMT2D controls a permissive chromatin state at Notch target genes. Nucleic Acids Res 2016; 44:4703-4720; PMID:26912830; http://dx.doi.org/10.1093/nar/gkw105
   PubMed Web of Science ®Google Scholar
• Mohan M, Herz HM, Shilatifard A. SnapShot: Histone lysine methylase complexes. Cell 2012; 149:498–498; ; http://dx.doi.org/10.1016/j.cell.2012.03.025
   Google Scholar
• Dephoure N, Zhou C, Villén J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP. A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A 2008; 105:10762-10767; PMID:18669648; http://dx.doi.org/10.1073/pnas.0805139105
   PubMed Web of Science ®Google Scholar
• Yoo JY, Choi HK, Choi KC, Park SY, Ota I, Yook JI, Lee YH, Kim K, Yoon HG. Nuclear hormone receptor corepressor promotes esophageal cancer cell invasion by transcriptional repression of interferon-gamma-inducible protein 10 in a casein kinase 2-dependent manner. Mol Biol Cell 2012; 23:2943-2954; PMID:22675025; http://dx.doi.org/10.1091/mbc.E11-11-0947
   PubMed Web of Science ®Google Scholar
• Jung C, Mittler G, Oswald F, Borggrefe T. RNA helicase Ddx5 and the noncoding RNA SRA act as coactivators in the Notch signaling pathway. Biochim Biophys Acta 2013; 1833:1180-1189; PMID: 23396200; http://dx.doi.org/10.1016/j.bbamcr.2013.01.032
   PubMed Web of Science ®Google Scholar
• Liefke R, Oswald F, Alvarado C, Ferres-Marco D, Mittler G, Rodriguez P, Dominguez M, Borggrefe T. Histone demethylase KDM5A is an integral part of the core Notch-RBP-J repressor complex. Genes Dev 2010; 24:590-601; PMID:20231316; http://dx.doi.org/10.1101/gad.563210
   PubMed Web of Science ®Google Scholar
• Mulligan P, Yang F, Di Stefano L, Ji JY, Ouyang J, Nishikawa JL, Toiber D, Kulkarni M, Wang Q, Najafi-Shoushtari SH et al. A SIRT1-LSD1 corepressor complex regulates Notch target gene expression and development. Mol Cell 2011; 42:689-699; PMID:21596603; http://dx.doi.org/10.1016/j.molcel.2011.04.020
   PubMed Web of Science ®Google Scholar
• Aguilar-Arnal L, Katada S, Orozco-Solis R, Sassone-Corsi, P. NAD(+)-SIRT1 control of H3K4 trimethylation through circadian deacetylation of MLL1. Nat Struct Mol Biol 2015; 22:312-318; PMID:25751424; http://dx.doi.org/10.1038/nsmb.2990
   PubMed Web of Science ®Google Scholar