Document Detail


Molecular Chaperone Activity and Biological Regulatory Actions of the TPR-Domain Immunophilins FKBP51 and FKBP52.
MedLine Citation:
PMID:  24694367     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
Immunophilins comprise a family of intracellular proteins with peptidyl-prolyl-(cis/trans)-isomerase activity. These foldases are abundant, ubiquitous, and able to bind immunosuppressant drugs, from which the term immunophilin derives. Family members are found in abundance in virtually all organisms and subcellular compartments, and their amino acid sequences are conserved phylogenetically. Immunophilins possess the ability to function as molecular chaperones favoring the proper folding and biological regulation of their biological actions. Their ability to interact via their TPR domains with the 90-kDa heat-shock protein, and through this chaperone, with several signalling cascade factors is of particular importance. Among the family members, the highly homologous proteins FKBP51 and FKBP52 were first characterized due to their ability to interact with steroid hormone receptors. Since then, much progress has been made in understanding the mechanisms by which they regulate receptor signaling and the resulting roles they play not only in endocrine processes, but also in cell architecture, neurodifferentiation, and tumor progression. In this article we review the most relevant features of these two immunophilins and their potential as pharmacologic targets.
Authors:
Alejandra G Erlejman; Mariana Lagadari; Diondra C Harris; Marc B Cox; Mario D Galigniana
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2014-3-31
Journal Detail:
Title:  Current protein & peptide science     Volume:  -     ISSN:  1875-5550     ISO Abbreviation:  Curr. Protein Pept. Sci.     Publication Date:  2014 Mar 
Date Detail:
Created Date:  2014-4-3     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  100960529     Medline TA:  Curr Protein Pept Sci     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
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