1 |
Ann, E.J., Kim, H.Y., Seo, M.S., Mo, J.S., Kim, M.Y., Yoon, J.H., Ahn, J.S., and Park, H.S. (2012). Wnt5a controls Notch1 signaling through CaMKII-mediated degradation of the SMRT corepressor protein. J. Biol. Chem. 287, 36814-36829.
DOI
|
2 |
Ariyoshi, M., and Schwabe, J.W. (2003). A conserved structural motif reveals the essential transcriptional repression function of Spen proteins and their role in developmental signaling. Genes Dev. 17, 1909-1920.
DOI
|
3 |
Borggrefe, T., and Oswald, F. (2009). The Notch signaling pathway: transcriptional regulation at Notch target genes. Cell. Mol. Life Sci. 66, 1631-1646.
DOI
|
4 |
Borggrefe, T., and Oswald, F. (2014). Keeping notch target genes off: a CSL corepressor caught in the act. Structure 22, 3-5.
DOI
|
5 |
Chen, J.D., and Evans, R.M. (1995). A transcriptional co-repressor that interacts with nuclear hormone receptors. Nature 377, 454-457.
DOI
|
6 |
Collins, K.J., Yuan, Z., and Kovall, R.A. (2014). Structure and function of the CSL-KyoT2 corepressor complex: a negative regulator of Notch signaling. Structure 22, 70-81.
DOI
|
7 |
Hsieh, J.J., Zhou, S., Chen, L., Young, D.B., and Hayward, S.D. (1999). CIR, a corepressor linking the DNA binding factor CBF1 to the histone deacetylase complex. Proc. Natl. Acad. Sci. USA 96, 23-28.
DOI
|
8 |
Huang, E.Y., Zhang, J., Miska, E.A., Guenther, M.G., Kouzarides, T., and Lazar, M.A. (2000). Nuclear receptor corepressors partner with class II histone deacetylases in a Sin3-independent repression pathway. Genes Dev. 14, 45-54.
|
9 |
Johnson, S.E., Ilagan, M.X., Kopan, R., and Barrick, D. (2010). Thermodynamic analysis of the CSL x Notch interaction: distribution of binding energy of the Notch RAM region to the CSL beta-trefoil domain and the mode of competition with the viral transactivator EBNA2. J. Biol. Chem. 285, 6681-6692.
DOI
|
10 |
Kao, H.Y., Ordentlich, P., Koyano-Nakagawa, N., Tang, Z., Downes, M., Kintner, C.R., Evans, R.M., and Kadesch, T. (1998). A histone deacetylase corepressor complex regulates the Notch signal transduction pathway. Genes Dev. 12, 2269-2277.
DOI
|
11 |
Kim, J.Y., Park, O.G., Lee, J.W., and Lee, Y.C. (2007). One- plus twohybrid system, a novel yeast genetic selection for specific missense mutations disrupting protein/protein interactions. Mol. Cell. Proteomics 6, 1727-1740.
DOI
|
12 |
Borggrefe, T., and Oswald, F. (2016). Setting the stage for notch: The Drosophila Su(H)-hairless repressor complex. PLoS Biol. 14, e1002524.
DOI
|
13 |
Kovall, R.A., and Hendrickson, W.A. (2004). Crystal structure of the nuclear effector of Notch signaling, CSL, bound to DNA. EMBO J. 23, 3441-3451.
DOI
|
14 |
Kim, J.Y., Park, O.G., and Lee, Y.C. (2012). One- plus two-hybrid system for the efficient selection of missense mutant alleles defective in protein-protein interactions. Methods Mol. Biol. 812, 209-223.
|
15 |
Kopan, R., and Ilagan, M.X. (2009). The canonical Notch signaling pathway: unfolding the activation mechanism. Cell 137, 216-233.
DOI
|
16 |
Kovall, R.A., and Blacklow, S.C. (2010). Mechanistic insights into Notch receptor signaling from structural and biochemical studies. Curr. Topics Dev. Biol. 92, 31-71.
|
17 |
Kumar, A., Huh, T.L., Choe, J., and Rhee, M. (2017). Rnf152 is essential for NeuroD expression and Delta-notch signaling in the zebrafish embryos. Mol. Cells 40, 945-953.
|
18 |
Mikami, S., Kanaba, T., Takizawa, N., Kobayashi, A., Maesaki, R., Fujiwara, T., Ito, Y., and Mishima, M. (2014). Structural insights into the recruitment of SMRT by the corepressor SHARP under phosphorylative regulation. Structure 22, 35-46.
DOI
|
19 |
Mottis, A., Mouchiroud, L., and Auwerx, J. (2013). Emerging roles of the corepressors NCoR1 and SMRT in homeostasis. Genes Dev. 27, 819-835.
DOI
|
20 |
Nam, Y., Sliz, P., Song, L., Aster, J.C., and Blacklow, S.C. (2006). Structural basis for cooperativity in recruitment of MAML coactivators to Notch transcription complexes. Cell 124, 973-983.
DOI
|
21 |
Oberoi, J., Fairall, L., Watson, P.J., Yang, J.C., Czimmerer, Z., Kampmann, T., Goult, B.T., Greenwood, J.A., Gooch, J.T., Kallenberger, B.C., et al. (2011). Structural basis for the assembly of the SMRT/NCoR core transcriptional repression machinery. Nat. Struct. Mol. Biol. 18, 177-184.
DOI
|
22 |
Tabaja, N., Yuan, Z., Oswald, F., and Kovall, R.A. (2017). Structurefunction analysis of RBP-J-interacting and tubulin-associated (RITA) reveals regions critical for repression of Notch target genes. J. Biol. Chem. 292, 10549-10563.
DOI
|
23 |
Oswald, F., Tauber, B., Dobner, T., Bourteele, S., Kostezka, U., Adler, G., Liptay, S., and Schmid, R.M. (2001). p300 acts as a transcriptional coactivator for mammalian Notch-1. Mol. Cell. Biol. 21, 7761-7774.
DOI
|
24 |
Oswald, F., Kostezka, U., Astrahantseff, K., Bourteele, S., Dillinger, K., Zechner, U., Ludwig, L., Wilda, M., Hameister, H., Knochel, W., et al. (2002). SHARP is a novel component of the Notch/RBP-Jkappa signalling pathway. EMBO J. 21, 5417-5426.
DOI
|
25 |
Pajerowski, A.G., Nguyen, C., Aghajanian, H., Shapiro, M.J., and Shapiro, V.S. (2009). NKAP is a transcriptional repressor of notch signaling and is required for T cell development. Immunity 30, 696-707.
DOI
|
26 |
VanderWielen, B.D., Yuan, Z., Friedmann, D.R., and Kovall, R.A. (2011). Transcriptional repression in the Notch pathway: thermodynamic characterization of CSL-MINT (Msx2-interacting nuclear target protein) complexes. J. Biol. Chem. 286, 14892-14902.
DOI
|
27 |
Yuan, Z., Praxenthaler, H., Tabaja, N., Torella, R., Preiss, A., Maier, D., and Kovall, R.A. (2016). Structure and function of the Su(H)-Hairless repressor complex, the major antagonist of notch signaling in Drosophila melanogaster. PLoS Biol. 14, e1002509.
DOI
|
28 |
Wacker, S.A., Alvarado, C., von Wichert, G., Knippschild, U., Wiedenmann, J., Clauss, K., Nienhaus, G.U., Hameister, H., Baumann, B., Borggrefe, T., et al. (2011). RITA, a novel modulator of Notch signalling, acts via nuclear export of RBP-J. EMBO J. 30, 43-56.
DOI
|
29 |
Wilson, J.J., and Kovall, R.A. (2006). Crystal structure of the CSLNotch-Mastermind ternary complex bound to DNA. Cell 124, 985-996.
DOI
|