Diverse structures, functions and uses of FK506 binding proteins

• Published in: Cellular signalling Vol. 38; pp. 97 - 105
• Main Authors: Bonner, Julia Maeve, Boulianne, Gabrielle L.
• Format: Journal Article
• Language: English
• Published: England Elsevier Inc 01-10-2017
• Subjects: Animals; FK506; FK506 binding protein (FKBP); Humans; Immunophilin; Models, Biological; Peptidylprolyl cis/trans isomerase; Protein Transport; Subcellular Fractions - metabolism; Tacrolimus Binding Proteins - chemistry; Tacrolimus Binding Proteins - metabolism; FK506; Peptidylprolyl cis/trans isomerase; FK506 binding protein (FKBP); Immunophilin
• ISSN: 0898-6568; 1873-3913
• DOI: 10.1016/j.cellsig.2017.06.013

FK506 (Tacrolimus), isolated from Streptomyces tsukubaenis is a powerful immunosuppressant shown to inhibit T cell activation. FK506 mediated immunosuppression requires the formation of a complex between FK506, a FK506 binding protein (FKBP) and calcineurin. Numerous FKBPs have been identified in a wide range of species, from single celled organisms to humans. FKBPs show peptidylprolyl cis/trans isomerase (PPIase) activity and have been shown to affect a wide range of cellular processes including protein folding, receptor signaling and apoptosis. FKBPs also affect numerous biological functions in addition to immunosuppression including regulation of cardiac function, neuronal function and development and have been implicated in several diseases including cardiac disease, cancer and neurodegenerative diseases such as Alzheimer's disease. More recently, FKBPs have proven useful as molecular tools for studying protein interactions, localization and functions. This review provides an overview of the current state of knowledge of FKBPs and their numerous biological functions and uses.
•FKBPs affect a wide range of cellular processes.•FKBPs play a key role in development and are implicated in several diseases.•FKBPs can be used as molecular tools to study protein function.