Journal
MOLECULAR CELL
Volume 30, Issue 4, Pages 507-518Publisher
CELL PRESS
DOI: 10.1016/j.molcel.2008.03.011
Keywords
-
Categories
Funding
- MRC [MC_U105192713, MC_U105178845, MC_U105184273] Funding Source: UKRI
- Medical Research Council [MC_U105184273, MC_U105192713, MC_U105178845] Funding Source: researchfish
- Cancer Research UK [C7379/A8709] Funding Source: Medline
- Medical Research Council [MC_U105192713, MC_U105184273, MC_U105178845] Funding Source: Medline
Ask authors/readers for more resources
Pygo and BCL9/Legless transduce the Wnt signal by promoting the transcriptional activity of beta-catenin/ Armadillo in normal and malignant cells. We show that human and Drosophila Pygo PHD fingers associate with their cognate HD1 domains from BCL9/Legless to bind specifically to the histone H3 tail methylated at lysine 4 (H3K4me). The crystal structures of ternary complexes between PHD, HD1, and two different H3K4me peptides reveal a unique mode of histone tail recognition: efficient histone binding requires HD1 association, and the PHD-HD1 complex binds preferentially to H3K4me2 while displaying insensitivity to methylation of H3R2. Therefore, this is a prime example of histone tail binding by a PHD finger (of Pygo) being modulated by a cofactor (BCL9/Legless). Rescue experiments in Drosophila indicate that Wnt signaling outputs depend on histone decoding. The specificity of this process provided by the Pygo-BCL9/Legless complex suggests that this complex facilitates an early step in the transition from gene silence to Wnt-induced transcription.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available