Immunophilins for the love of proteins

Authors: S Barik

Publish Date: 2006/10/31

Volume: 63, Issue: 24, Pages: 2889-2900

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Abstract

Immunophilins are chaperones that may also exhibit peptidylprolyl isomerase PPIase activity This review summarizes our knowledge of the two largest families of immunophilins namely cyclophilin and FK506binding protein and a novel chimeric dualfamily immunophilin named FK506 and cyclosporinbinding protein FCBP The larger members of each family are modular in nature consisting of multiple PPIase and/or proteinprotein interaction domains Despite the apparent difference in their sequence and threedimensional structure the three families encode similar enzymatic and biological functions Recent studies have revealed that many immunophilins possess a chaperone function independent of PPIase activity Knockout animal studies have confirmed multiple essential roles of immunophilins in physiology and development An immunophilin is indeed a natural ‘proteinphilin’ Greek ‘philin’ = friend that interacts with proteins to guide their proper folding and assembly

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