FK506-binding protein like (None)

FKBPL (FK506-binding protein like) is a divergent member of the immunophilin protein superfamily. While it shares homology with FK506-binding proteins (FKBPs), FKBPL notably lacks peptidyl-prolyl isomerase (PPIase) activity. FKBPL retains a PPI domain and contains a tetratricopeptide repeat (TPR) domain that facilitates protein-protein interactions, particularly as part of multi-protein complexes. It acts as a co-chaperone within steroid hormone receptor complexes by associating with Hsp90 via its TPR domain, regulating steroid receptor signaling pathways. FKBPL exhibits anti-tumor activity by inhibiting angiogenesis and cancer stemness. Recent studies highlight FKBPL’s role in maintaining vascular integrity and regulating inflammation through modulation of NFκB signaling. Variants near or within the *FKBPL* gene are associated with inflammatory disorders. FKBPL influences estrogen receptor signaling—affecting response to drugs such as tamoxifen used in breast cancer therapy.

Other names

FKBPLDIR1NG7WISP39FKBP4FKBP prolyl isomerase like

Inhibition of angiogenesis and cancer stemness; modulation of NFκB signaling; regulation of steroid receptor/Hsp90 complex