Regulatory role of the 90-kDa-heat-shock protein (Hsp90) and associated factors on gene expression

NF-κB Transcriptional Activity Is Modulated by FK506-binding Proteins FKBP51 and FKBP52

“…This is confirmed by the fact that point mutants in the TPR domains of the FKBPs unable to bind Hsp90 show similar effects as the wild type immunophilins. Nevertheless, the overexpression of a TPR peptide inhibits the biological action of both proteins, suggesting that the domain itself is required at some point in the mechanism of action, perhaps for interacting with other regulatory factors such as cofactors (53). On the other hand, the PPIase activity of FKBP52 is very important for its stimulatory action, although this enzymatic activity is not required for the FKBP51 inhibitory action.…”

Geranylgeranylacetone protects against cerebral ischemia and reperfusion injury: HSP90 and eNOS phosphorylation involved

“…To explore the molecular mechanism of GGA action, unlike the previous studies, we focused on hsp90, another HSP induced by GGA, and eNOS, an important cerebrovascular Hsp90, an adenosine triphosphate-dependent chaperone, is the major soluble protein of the cell. It accounts for 2% of the total soluble proteins in resting cells and up to 10% in stressed cells where it performs the cytoprotective function (Erlejman et al, 2014). Hsp90 is essential for various cellular processes, such as protein folding, protein degradation and signal transduction cascades.…”

Functions of the Hsp90-Binding FKBP Immunophilins

“…Like other Hsp90-associated FKBP proteins, FKBPL also forms complexes with various steroid hormone receptors (reviewed in Erlejman et al 2014). FK-BPL and Hsp90 appear to stabilize AR, ER, and GR/Hsp90 complexes (Sunnotel et al 2010;McKeen et al 2008;McKeen et al 2010).…”