Formation of the MLL2 complex

Stable Identifier
R-HSA-9676255
Type
Reaction [binding]
Species
Homo sapiens
Compartment
ReviewStatus
5/5
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Cleaved KMT2B (also known as MLL2) dimers bind the WRAD complex, consisting of WDR5, RBBP5, ASH2L and DPY30, to form the MLL2 complex. WDR5 plays an important role in the optimal stimulation of MLL2 methyltransferase activity by the RBBP5:ASH2L heterodimer (Zhang et al. 2012, Jiang et al. 2013, Wei et al. 2021; Mayse et al. 2022).

MLL2 complex is responsible for H3K4 trimethylation (H3K4me3) on specific gene promotors and cis-regulatory sites (Jiang et al. 2013). These modifications play a role in regulating bivalent developmental genes and regulators involved in primordial germ cell specification during embryonic stem cell differentiation (reviewed in Klonou et al. 2021).
Literature References
PubMed ID Title Journal Year
35190547 Disentangling the recognition complexity of a protein hub using a nanopore

Mayse, LA, Imran, A, Larimi, MG, Cosgrove, MS, Wolfe, AJ, Movileanu, L

Nat Commun 2022
23995757 Regulation of transcription by the MLL2 complex and MLL complex-associated AKAP95

Jiang, H, Lu, X, Shimada, M, Dou, Y, Tang, Z, Roeder, RG

Nat Struct Mol Biol 2013
34933446 GRWD1-WDR5-MLL2 Epigenetic Complex Mediates H3K4me3 Mark and Is Essential for Kaposi's Sarcoma-Associated Herpesvirus-Induced Cellular Transformation

Wei, S, Lu, S, Liang, L, Wang, X, Li, W, Li, T, Chen, L, Ju, E, Zhang, X, Lai, Z, Huang, Y, Lu, X, Gao, SJ

mBio 2021
22266653 The plasticity of WDR5 peptide-binding cleft enables the binding of the SET1 family of histone methyltransferases

Zhang, P, Lee, H, Brunzelle, JS, Couture, JF

Nucleic Acids Res. 2012
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