Peptidyl-prolyl cis-trans isomerase FKBP8

Definition:

Constitutively inactive PPiase, which becomes active when bound to calmodulin and calcium. Seems to act as a chaperone for BCL2, targets it to the mitochondria and modulates its phosphorylation state. The BCL2/FKBP8/calmodulin/calcium complex probably interferes with the binding of BCL2 to its targets. The active form of FKBP8 may therefore play a role in the regulation of apoptosis. Involved in the inhibition of viral infection by influenza A viruses (IAV).

References:

[1]. Matthias Weiwad, et al. A reassessment of the inhibitory capacity of human FKBP38 on calcineurin. FEBS Lett. 2005 Mar 14;579(7):1591-6. [Content Brief]

[2]. Michiko Shirane, et al. Inherent calcineurin inhibitor FKBP38 targets Bcl-2 to mitochondria and inhibits apoptosis. Nat Cell Biol. 2003 Jan;5(1):28-37. [Content Brief]

[3]. Lingyan Wang, et al. Comparative influenza protein interactomes identify the role of plakophilin 2 in virus restriction. Nat Commun. 2017 Feb 7;8:13876. [Content Brief]

[4]. Cong Bao Kang, et al. Molecular characterization of FK-506 binding protein 38 and its potential regulatory role on the anti-apoptotic protein Bcl-2. Biochem Biophys Res Commun. 2005 Nov 11;337(1):30-8. [Content Brief]

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