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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
4
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pubmed:dateCreated |
2008-5-23
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pubmed:abstractText |
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.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/18498752-10921899,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18498752-11057903,
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Proteins, Signal Transducing,
http://linkedlifedata.com/resource/pubmed/chemical/BCL9 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Drosophila Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Histones,
http://linkedlifedata.com/resource/pubmed/chemical/Intracellular Signaling Peptides...,
http://linkedlifedata.com/resource/pubmed/chemical/Lysine,
http://linkedlifedata.com/resource/pubmed/chemical/Multiprotein Complexes,
http://linkedlifedata.com/resource/pubmed/chemical/Neoplasm Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/PYGO1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Wnt Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/legless protein, Drosophila,
http://linkedlifedata.com/resource/pubmed/chemical/pygopus protein, Drosophila
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
1097-4164
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
23
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pubmed:volume |
30
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
507-18
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:18498752-Adaptor Proteins, Signal Transducing,
pubmed-meshheading:18498752-Amino Acid Sequence,
pubmed-meshheading:18498752-Animals,
pubmed-meshheading:18498752-Binding Sites,
pubmed-meshheading:18498752-Crystallography, X-Ray,
pubmed-meshheading:18498752-Drosophila Proteins,
pubmed-meshheading:18498752-Drosophila melanogaster,
pubmed-meshheading:18498752-Histones,
pubmed-meshheading:18498752-Humans,
pubmed-meshheading:18498752-Intracellular Signaling Peptides and Proteins,
pubmed-meshheading:18498752-Lysine,
pubmed-meshheading:18498752-Methylation,
pubmed-meshheading:18498752-Models, Molecular,
pubmed-meshheading:18498752-Molecular Sequence Data,
pubmed-meshheading:18498752-Multiprotein Complexes,
pubmed-meshheading:18498752-Neoplasm Proteins,
pubmed-meshheading:18498752-Peptides,
pubmed-meshheading:18498752-Protein Binding,
pubmed-meshheading:18498752-Protein Conformation,
pubmed-meshheading:18498752-Recombinant Fusion Proteins,
pubmed-meshheading:18498752-Sequence Alignment,
pubmed-meshheading:18498752-Signal Transduction,
pubmed-meshheading:18498752-Wnt Proteins
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pubmed:year |
2008
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pubmed:articleTitle |
Decoding of methylated histone H3 tail by the Pygo-BCL9 Wnt signaling complex.
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pubmed:affiliation |
MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 0QH, UK.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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