High impact information on FKBP59

• Likewise, purified recombinant dFKBP59 produced a graded inhibition of TRPL single channel activity in excised inside-out patches when added to the cytoplasmic membrane surface [1].
• Immunoprecipitations from Drosophila S2 cells and from fly head lysates demonstrated that dFKBP59, but not dFKBP12, interacts with TRPL in vivo [1].
• Likewise, INAD immunoprecipitates with dFKBP59 from S2 cell and head lysates [1].
• Expression of dFKBP59 produced an inhibition of Ca(2+) influx via TRPL in fura-2 assays [1].
• Northern hybridization reveals that the dFKBP59 mRNA is expressed throughout the Drosophila life-cycle [2].

Biological context of FKBP59

• Finally, I have mapped an enhancer trap element within the 5' region of dFKBP59 which may help in future studies to address the question of its function during Drosophila development [2].
• The predicted amino acid sequence of this cDNA shows that the dFKBP59 protein contains one highly conserved FKBP12-like domain followed by two others with less conservation [2].

Analytical, diagnostic and therapeutic context of FKBP59

• Immunoprecipitations from Sf9 cell lysates using recombinant tagged dFKBP59 and TRPL showed that these proteins directly interact with each other and with INAD [1].
• Addition of FK506 prior to immunoprecipitation resulted in a temperature-dependent dissociation of dFKBP59 and TRPL [1].
• Site-directed mutagenesis showed that mutations of P702Q or P709Q in the highly conserved TRPL sequence (701)LPPPFNVLP(709) eliminated interaction of the TRPL with dFKBP59 [1].
• In contrast to its mammalian homologs, in situ hybridization detected dFKBP59 expression in specific tissues: the lymph glands, Garland cells and oenocyte cells, which are all specialized tissues in which intensive exocytic/endocytic cycling takes place [2].
• Molecular cloning and embryonic expression of dFKBP59, a novel Drosophila FK506-binding protein [2].

References