Premium
XAP2 inhibits glucocorticoid receptor activity in mammalian cells
Author(s) -
Laenger Anna,
Lang-Rollin Isabelle,
Kozany Christian,
Zschocke Jürgen,
Zimmermann Nicole,
Rüegg Joëlle,
Holsboer Florian,
Hausch Felix,
Rein Theo
Publication year - 2009
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2009.03.072
Subject(s) - glucocorticoid receptor , hsp90 , fkbp , chemistry , microbiology and biotechnology , receptor , glucocorticoid , nuclear receptor , biology , biochemistry , heat shock protein , transcription factor , endocrinology , gene
XAP2 is member of a protein family sharing the TPR protein interaction motif. It displays close homology to the immunophilins FKBP51 and FKBP52 that act via the Hsp90 folding machinery to regulate the glucocorticoid receptor (GR). We show that XAP2 inhibits GR by reducing its responsiveness to hormone in transcriptional activation. The effect of XAP2 on GR requires its interaction with Hsp90 through the TPR motif. The PPIase‐like region turned out to be enzymatically inactive. Thus, PPIase activity is not essential for the action of XAP2 on GR, similarly to FKBP51 and FKBP52.