Journal
MOLECULAR AND CELLULAR BIOLOGY
Volume 21, Issue 10, Pages 3589-3597Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/MCB.21.10.3589-3597.2001
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- NCI NIH HHS [R01 CA38725] Funding Source: Medline
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The PHD fingers of the human MLL and Drosophila trx proteins have strong amino acid sequence conservation but their function is unknown. We have determined that these fingers mediate homodimerization and binding of MLL to Cyp33, a nuclear cyclophilin. These two proteins interact in vitro and in vivo in mammalian cells and colocalize at specific nuclear subdomains. Overexpression of the Cyp33 protein in leukemia cells results in altered expression of HOK genes that are targets for regulation by MLL. These alterations are suppressed by cyclosporine and are not observed in cell lines that express a mutant MLL protein without PHD fingers. These results suggest that binding of Cyp33 to MLL modulates its effects on the expression of target genes.
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