| Disorders in protein conformation that show effects on ER function
are the basis of many sporadic and inherited diseases. FKBP, which is a protein
from the immunophilin group that has an affinity to FK506 drugs and antibiotics,
functions as a chaperone and is involved in protein folding and cargo in the
ER. We studied FKBP in Drosophila egg chambers as a model system and saw expression
in the dorsal anterior region. Overexpression of FKBP has defects in dorsal
appendage patterning. In addition, we have produced loss-of-function FKBP mosaics
to determine which pathways are affected when FKBP is defective and found that
follicle cell clones in stage 9 egg chambers show Notch mislocalization. This
suggests that FKBP might be involved in the transportation of Notch from the
ER. We are in the process of analyzing this cell biological function of FKBP
in more detail. |