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http://purl.uniprot.org/citations/20541251http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20541251http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20541251http://www.w3.org/2000/01/rdf-schema#comment"The MLL1 gene is a frequent target for recurrent chromosomal translocations, resulting in transformation of hematopoietic precursors into leukemia stem cells. Here, we report on structure-function studies that elucidate molecular events in MLL1 binding of histone H3K4me3/2 marks and recruitment of the cyclophilin CyP33. CyP33 contains a PPIase and a RRM domain and regulates MLL1 function through HDAC recruitment. We find that the PPIase domain of CyP33 regulates the conformation of MLL1 through proline isomerization within the PHD3-Bromo linker, thereby disrupting the PHD3-Bromo interface and facilitating binding of the MLL1-PHD3 domain to the CyP33-RRM domain. H3K4me3/2 and CyP33-RRM target different surfaces of MLL1-PHD3 and can bind simultaneously to form a ternary complex. Furthermore, the MLL1-CyP33 interaction is required for repression of HOXA9 and HOXC8 genes in vivo. Our results highlight the role of PHD3-Bromo cassette as a regulatory platform, orchestrating MLL1 binding of H3K4me3/2 marks and cyclophilin-mediated repression through HDAC recruitment."xsd:string
http://purl.uniprot.org/citations/20541251http://purl.org/dc/terms/identifier"doi:10.1016/j.cell.2010.05.016"xsd:string
http://purl.uniprot.org/citations/20541251http://purl.org/dc/terms/identifier"doi:10.1016/j.cell.2010.05.016"xsd:string
http://purl.uniprot.org/citations/20541251http://purl.uniprot.org/core/author"Li H."xsd:string
http://purl.uniprot.org/citations/20541251http://purl.uniprot.org/core/author"Li H."xsd:string
http://purl.uniprot.org/citations/20541251http://purl.uniprot.org/core/author"Song J."xsd:string
http://purl.uniprot.org/citations/20541251http://purl.uniprot.org/core/author"Song J."xsd:string
http://purl.uniprot.org/citations/20541251http://purl.uniprot.org/core/author"Wang Z."xsd:string
http://purl.uniprot.org/citations/20541251http://purl.uniprot.org/core/author"Wang Z."xsd:string
http://purl.uniprot.org/citations/20541251http://purl.uniprot.org/core/author"Patel D.J."xsd:string
http://purl.uniprot.org/citations/20541251http://purl.uniprot.org/core/author"Patel D.J."xsd:string
http://purl.uniprot.org/citations/20541251http://purl.uniprot.org/core/author"Allis C.D."xsd:string
http://purl.uniprot.org/citations/20541251http://purl.uniprot.org/core/author"Allis C.D."xsd:string
http://purl.uniprot.org/citations/20541251http://purl.uniprot.org/core/author"Wang G.G."xsd:string
http://purl.uniprot.org/citations/20541251http://purl.uniprot.org/core/author"Wang G.G."xsd:string
http://purl.uniprot.org/citations/20541251http://purl.uniprot.org/core/author"Milne T.A."xsd:string
http://purl.uniprot.org/citations/20541251http://purl.uniprot.org/core/author"Milne T.A."xsd:string
http://purl.uniprot.org/citations/20541251http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20541251http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20541251http://purl.uniprot.org/core/name"Cell"xsd:string
http://purl.uniprot.org/citations/20541251http://purl.uniprot.org/core/name"Cell"xsd:string
http://purl.uniprot.org/citations/20541251http://purl.uniprot.org/core/pages"1183-1194"xsd:string
http://purl.uniprot.org/citations/20541251http://purl.uniprot.org/core/pages"1183-1194"xsd:string