Peptidyl-prolyl cis-trans isomerase FKBP10 (FKBP10)

Peptidyl-prolyl cis-trans isomerase FKBP10 (FKBP10) is an enzyme of the FKBP-type immunophilin family localized to the endoplasmic reticulum. It functions as a molecular chaperone involved in the processing and proper folding of collagen and elastin, facilitating their cross-linking in the extracellular matrix. FKBP10 catalyzes the cis-trans isomerization of proline residues in target proteins, a critical step in collagen maturation. Mutations in FKBP10 cause connective tissue disorders including osteogenesis imperfecta and Bruck syndrome, characterized by bone fragility and joint contractures. Altered FKBP10 expression has also been linked to roles in cancer cell proliferation and invasion, likely via signaling pathways such as PI3K. FKBP10 can theoretically be targeted by immunosuppressive drugs like FK506 (tacrolimus) due to its similarity with other FKBP-type proteins, although it does not appear to be a major direct therapeutic target at present[1][2][5][6].

Other names

65 kDa FK506-binding protein65 kDa FKBPFK506-binding protein 10FKBP-10FKBP-65FKBP65FKBP6hFKBP65immunophilin FKBP65PPIase FKBP10rotamaseFLJ20683FLJ22041FLJ23833OI11OI6PPIASE

Inhibition of peptidyl-prolyl cis-trans isomerase activity (by FK506 and similar immunosuppressive agents); Interference with collagen cross-linking