Evidence for a functional interaction between calmodulin and the glucocorticoid receptor.
Evidence for a functional interaction between calmodulin and the glucocorticoid receptor.
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DOI：
10.1006/bbrc.1995.1303
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发表时间：
1995-03
影响因子：
3.1
通讯作者：
Y. Ning;E. R. Sánchez
中科院分区：
文献类型：
--
作者：
Y. Ning;E. R. Sánchez
在膜结合受体的信号级联中，钙调蛋白（calmodulin, CaM）起着重要的作用。然而，CaM在细胞内类固醇受体激活中的作用知之甚少，这些受体被认为是配体调节的转录因子。我们在这里报道，CaM可以钙依赖的方式与含有hsp90的未转化糖皮质激素受体（GR）复合物相互作用。此外，我们证明了四种不相关的CaM拮抗剂（三氟拉嗪、化合物48/80、W7和phenoxybenzamine）在稳定转染MMTV-CAT报告基因的小鼠L929细胞中可以抑制gr介导的基因表达。这些结果证明CaM可能在类固醇激素受体的信号转导通路中发挥重要作用。
In the signaling cascade of membrane-bound receptors, calmodulin (CaM) plays an important role. However, little is known about the role of CaM in the activation of intracellular steroid receptors, which are known to act as ligand-regulated transcription factors. We report here that CaM can interact in a calcium-dependent manner with the untransformed glucocorticoid receptor (GR) complex containing hsp90. In addition, we demonstrate that four unrelated CaM antagonists (trifluoperazine, compound 48/80, W7, and phenoxybenzamine) can inhibit GR-mediated gene expression in mouse L929 cells stably-transfected with the MMTV-CAT reporter gene. These results provide evidence that CaM may play an important role in the signal transduction pathways of steroid hormone receptors.