XAP2抑制哺乳动物细胞中的糖皮质激素受体活性。
XAP2 inhibits glucocorticoid receptor activity in mammalian cells.
作者信息
Laenger Anna, Lang-Rollin Isabelle, Kozany Christian, Zschocke Jürgen, Zimmermann Nicole, Rüegg Joëlle, Holsboer Florian, Hausch Felix, Rein Theo
机构信息
Max Planck Institute of Psychiatry, Kraepelinstrasse 10, 80804 Munich, Germany.
出版信息
FEBS Lett. 2009 May 6;583(9):1493-8. doi: 10.1016/j.febslet.2009.03.072. Epub 2009 Apr 16.
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.
XAP2是一个共享TPR蛋白相互作用基序的蛋白质家族成员。它与通过Hsp90折叠机制调节糖皮质激素受体（GR）的免疫亲和素FKBP51和FKBP52显示出密切的同源性。我们发现，XAP2通过降低GR在转录激活中对激素的反应性来抑制GR。XAP2对GR的作用需要其通过TPR基序与Hsp90相互作用。结果表明，类肽基脯氨酰异构酶（PPIase）区域没有酶活性。因此，与FKBP51和FKBP52类似，PPIase活性对于XAP2对GR的作用并非必不可少。
Zotero 插件