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Free keywords:
MAJOR DEPRESSIVE DISORDER; HEAT-SHOCK-PROTEIN;
POSTTRAUMATIC-STRESS-DISORDER; PROLYL ISOMERASE DOMAIN; DIET-INDUCED
OBESITY; EARLY-LIFE STRESS; MOLECULAR CHAPERONE; ANTIDEPRESSANT
TREATMENT; PROGESTERONE-RECEPTOR; IMMUNOPHILIN FKBP51Biochemistry & Molecular Biology; Chemistry; chaperone; glucocorticoid receptor; FKBP51; FKBP5; signaling pathway;
drug;
Abstract:
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.
