FKBP family proteins : immunophilins with versatile biological functions

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FKBP family proteins : immunophilins with versatile biological functions

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dc.contributor.author Kang, Cong Bao
dc.contributor.author Ye, Hong
dc.contributor.author Dhe-Paganon, Sirano
dc.contributor.author Yoon, Ho Sup
dc.date.accessioned 2012-08-21T06:54:35Z
dc.date.available 2012-08-21T06:54:35Z
dc.date.copyright 2008
dc.date.issued 2012-08-21
dc.identifier.citation Kang, C. B., Ye, H., Dhe-Paganon, S., & Yoon, H. S. (2008). FKBP family proteins : immunophilins with versatile biological functions. Neurosignals, 16(4), 318–325.
dc.identifier.uri http://hdl.handle.net/10220/8409
dc.description.abstract Immunophilins consist of a family of highly conserved proteins binding with immunosuppressive drugs such as FK506, rapamycin and cyclosporin A. FK506-binding protein (FKBP) is one of two major immunophilins and most of FKBP family members bind FK506 and show peptidylprolyl cis/trans isomerase (PPIase) activity. Small size FKBP family members contain only FK506-binding domain, while FKBPs with large molecular weights possess extra domains such as tetratricopeptide repeat domains, calmodulin binding and transmembrane motifs. FKBPs are involved in several biochemical processes including protein folding, receptor signaling, protein trafficking and transcription. FKBP family proteins play important functional roles in the T-cell activation, when complexed with their ligands. The roles of immunophilins in protein transportation and apoptosis through their molecular interactions with receptors or proteins have emerged recently. Moreover, therapeutic implications of immunophilin ligands in treating neurodegenerative disorders have been accumulating. FK506 and its derivatives with no immunosuppressive activities bind to the conserved active sites of the canonical FKBP members such as FKBP12, which shows PPIase activity. These immunophilin ligands show variable efficacy in animal models for Parkinson’s disease, dementia, and spinal cord injury, where the canonical immunophilins function as chaperones and are associate with the protein folding and modulation of oxidative stress. On the other hand, in the noncanonical FKBP members such as FKBP38, FK506-binding site is not conserved and shows neither PPIase activity nor affinity to FK506. Interestingly, the small molecule- mediated inhibition of the noncanonical member of FKBP family appears to cause neuronal protection and induce proliferation of neuronal stem cells in a rat focal cerebral ischemia model. Currently, the mechanisms of actions remain unclear. This review focuses on molecular characteristics of the canonical and noncanonical FKBP family members and the biological functions of their ligands in performing neuroprotective and neurotrophic activities.
dc.language.iso en
dc.relation.ispartofseries Neurosignals
dc.rights © 2008 S. Karger AG, Basel. This is the author created version of a work that has been peer reviewed and accepted for publication by Neurosignals, S. Karger AG, Basel. It incorporates referee’s comments but changes resulting from the publishing process, such as copyediting, structural formatting, may not be reflected in this document. The published version is available at: http://dx.doi.org/10.1159/000123041.
dc.subject DRNTU::Science::Biological sciences.
dc.title FKBP family proteins : immunophilins with versatile biological functions
dc.type Journal Article
dc.contributor.school School of Biological Sciences
dc.identifier.doi http://dx.doi.org/10.1159/000123041
dc.description.version Accepted version

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