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Current Molecular Pharmacology

Editor-in-Chief

ISSN (Print): 1874-4672
ISSN (Online): 1874-4702

FK506-Binding Proteins and Their Diverse Functions

Author(s): Mingming Tong and Yu Jiang

Volume 9 , Issue 1 , 2016

Page: [48 - 65] Pages: 18

DOI: 10.2174/1874467208666150519113541

Price: $65

Abstract

FK506 binding proteins (FKBPs) are a family of highly conserved proteins in eukaryotes. The prototype of this protein family, FKBP12, is the binding partner for immunosuppressive drugs FK506 and rapamycin. FKBP12 functions as a cis/trans peptidyl prolyl isomerase (PPIase) that catalyzes interconversion between prolyl cis/trans conformations. Members of the FKBP family contain one or several PPIase domains, which do not always exhibit PPIase activity yet are all essential for their function. FKBPs are involved in diverse cellular functions including protein folding, cellular signaling, apoptosis and transcription. They elicit their function through direct binding and altering conformation of their target proteins, hence acting as molecular switches. In this review, we provide a general summary for the structures and diverse functions of FKBPs found in mammalian cells.

Keywords: Calcineurin, FK506, FK506 binding proteins, immunophilin, mTOR, peptidyl prolyl cis/trans isomerase.

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