2vpd
Decoding of methylated histone H3 tail by the Pygo-BCL9 Wnt signaling complexDecoding of methylated histone H3 tail by the Pygo-BCL9 Wnt signaling complex
Structural highlights
FunctionPYGO1_HUMAN Involved in signal transduction through the Wnt pathway. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedPygo 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. Decoding of methylated histone H3 tail by the Pygo-BCL9 Wnt signaling complex.,Fiedler M, Sanchez-Barrena MJ, Nekrasov M, Mieszczanek J, Rybin V, Muller J, Evans P, Bienz M Mol Cell. 2008 May 23;30(4):507-18. PMID:18498752[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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