Formation of the WRAD complex

Stable Identifier
Reaction [binding]
Homo sapiens
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WDR5 and DPY30 interact with the RBBP5:ASH2L heterodimer and together form the WRAD complex, which functions as a core subcomplex of all mammalian KMT2 histone methyltransferase complexes (Cho et al. 2007, Patel et al. 2011, Shinsky et al. 2015, reviewed by Ernst and Vakoc 2012). WDR5 directly interacts with RBBP5 (Odho et al. 2010), while DPY30 directly binds to ASH2L (Cho et al. 2007). RBBP5, ASH2L, and DPY30 may form a subcomplex prior to WDR5 binding (van Nuland et al. 2013). Based on stoichiometric analysis, DPY30 likely exists as a homo-oligomer in the WRAD complex (van Nuland et al. 2013).
Literature References
PubMed ID Title Journal Year
23508102 Quantitative dissection and stoichiometry determination of the human SET1/MLL histone methyltransferase complexes

Pallaki, P, Smits, AH, van Nuland, R, Jansen, PW, Timmers, HT, Vermeulen, M

Mol Cell Biol 2013
17500065 PTIP associates with MLL3- and MLL4-containing histone H3 lysine 4 methyltransferase complex

Ge, K, Guo, H, Hong, S, Hong, T, Yu, H, Copeland, TD, Kim, D, Dressler, GR, Guszczynski, T, Cho, YW, Kalkum, M

J. Biol. Chem. 2007
21106533 A novel non-SET domain multi-subunit methyltransferase required for sequential nucleosomal histone H3 methylation by the mixed lineage leukemia protein-1 (MLL1) core complex

Patel, A, Vought, VE, Cosgrove, MS, Dharmarajan, V

J. Biol. Chem. 2011
25561738 Biochemical reconstitution and phylogenetic comparison of human SET1 family core complexes involved in histone methylation

Cosgrove, MS, Viggiano, S, Shinsky, SA, Monteith, KE

J. Biol. Chem. 2015
20716525 Characterization of a novel WDR5-binding site that recruits RbBP5 through a conserved motif to enhance methylation of histone H3 lysine 4 by mixed lineage leukemia protein-1

Wilson, JR, Southall, SM, Odho, Z

J Biol Chem 2010
22652693 WRAD: enabler of the SET1-family of H3K4 methyltransferases

Ernst, P, Vakoc, CR

Brief Funct Genomics 2012
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