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XAP2 inhibits glucocorticoid receptor activity in mammalian cells.
Laenger, Anna; Lang-Rollin, Isabelle; Kozany, Christian; Zschocke, Jürgen; Zimmermann, Nicole; Rüegg, Joëlle; Holsboer, Florian; Hausch, Felix; Rein, Theo.
Afiliação
  • Laenger A; Max Planck Institute of Psychiatry, Kraepelinstrasse 10, 80804 Munich, Germany.
FEBS Lett ; 583(9): 1493-8, 2009 May 06.
Article em En | MEDLINE | ID: mdl-19375531
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.
Assuntos

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Receptores de Glucocorticoides / Peptídeos e Proteínas de Sinalização Intracelular Limite: Humans Idioma: En Ano de publicação: 2009 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Receptores de Glucocorticoides / Peptídeos e Proteínas de Sinalização Intracelular Limite: Humans Idioma: En Ano de publicação: 2009 Tipo de documento: Article