Publications by authors named "Wesley B Denny"
Article Synopsis
- FK506-binding proteins FKBP51 and FKBP52 are crucial for the function of the glucocorticoid receptor (GR), affecting its activity through their specific domains.
- The squirrel monkey serves as a model for glucocorticoid resistance due to overexpression of FKBP51, which results in low GR affinity and demonstrates a much stronger effect compared to human FKBP51.
- Research revealed that the TPR domain is essential for GR inhibition while the PPIase activity is not, with both FK1 and FK2 domains in squirrel monkey FKBP51 contributing significantly to its potent inhibitory effects.
FKBP52 is a widely expressed FK506-binding immunophilin that possesses peptidylprolyl isomerase activity and a tetratricopeptide repeat involved in protein-protein interaction. FKBP52 plays an important role in steroid receptor function and is implicated in other diverse processes, including regulation of transcription, cation channel activity, and gene transfer efficiency. Reported here is the genomic organization of the human FKBP52 gene (FKBP4), which shares all but one of the same exon-intron boundaries as the structurally related immunophilin FKBP51 gene (FKBP5).
View Article and Find Full Text PDFFKBP51 and FKBP52 are large molecular weight FK506-binding immunophilins that have diverse biochemical functions. Best studied is the role that they play as components of steroid hormone receptors. Differential display and gene array screens have identified FKBP51 as a progestin-inducible gene.
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