Peptidyl-prolyl cis-trans isomerase FKBP8 (FKBP8)

Peptidyl-prolyl cis-trans isomerase FKBP8 (FKBP8) is a member of the immunophilin protein family, encoded by the FKBP8 gene in humans. While structurally related to other FKBP proteins, FKBP8 is unusual in that it lacks classic peptidyl-prolyl isomerase (PPIase) activity unless activated by calcium-bound calmodulin, acting instead largely as a chaperone. FKBP8 forms complexes with BCL2 protein and calmodulin, helping regulate mitochondrial localization and phosphorylation status of BCL2, thereby modulating apoptosis in cells. FKBP8 is also implicated in cellular protein folding, trafficking, and immune regulation, with roles in neuronal processes and memory. Disease associations include cancer, viral infections (such as hepatitis C and influenza A), and certain germinomas[1][2][3][6]. FKBP8 is known to interact with the immunosuppressive drug tacrolimus (FK506), though its distinct mechanism limits classic immunosuppressive activity observed in other FKBPs[3][6].

Other names

FK506-binding protein 8FKBP38Rotamase38 kDa FKBPFKBP-38FKBP-8hFKBP38FKBPr38FKBPR38FK506 binding protein 8PPIase FKBP8

Inhibition of protein interactions via FK506-binding, Potential modulation of apoptosis via BCL2 pathway chaperoning