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Int. J. Mol. Sci. 2017, 18(12), 2614;

The FKBP51 Glucocorticoid Receptor Co-Chaperone: Regulation, Function, and Implications in Health and Disease

Translational Psychiatry Program, Department of Psychiatry and Behavioral Sciences, McGovern Medical School, The University of Texas Health Science Center at Houston, Houston, TX 77054, USA
Department of Translational Science in Psychiatry, Max Planck Institute of Psychiatry, 80804 Munich, Germany
Authors to whom correspondence should be addressed.
Received: 30 October 2017 / Revised: 21 November 2017 / Accepted: 29 November 2017 / Published: 5 December 2017
(This article belongs to the Section Biochemistry)
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Among the chaperones and co-chaperones regulating the glucocorticoid receptor (GR), FK506 binding protein (FKBP) 51 is the most intensely investigated across different disciplines. This review provides an update on the role of the different co-chaperones of Hsp70 and Hsp90 in the regulation of GR function. The development leading to the focus on FKBP51 is outlined. Further, a survey of the vast literature on the mechanism and function of FKBP51 is provided. This includes its structure and biochemical function, its regulation on different levels—transcription, post-transcription, and post-translation—and its function in signaling pathways. The evidence portraying FKBP51 as a scaffolding protein organizing protein complexes rather than a chaperone contributing to the folding of individual proteins is collated. Finally, FKBP51’s involvement in physiology and disease is outlined, and the promising efforts in developing drugs targeting FKBP51 are discussed. View Full-Text
Keywords: chaperone; glucocorticoid receptor; FKBP51; FKBP5; signaling pathway; drug chaperone; glucocorticoid receptor; FKBP51; FKBP5; signaling pathway; drug

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Fries, G.R.; Gassen, N.C.; Rein, T. The FKBP51 Glucocorticoid Receptor Co-Chaperone: Regulation, Function, and Implications in Health and Disease. Int. J. Mol. Sci. 2017, 18, 2614.

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