RanBP10 acts as a novel coactivator for the androgen receptor
RanBP10 acts as a novel coactivator for the androgen receptor
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DOI：
10.1016/j.bbrc.2008.01.072
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发表时间：
2008-03-28
影响因子：
3.1
通讯作者：
Inui, Hiroshi
中科院分区：
文献类型：
--
作者：
Harada, Naoki;Yokoyama, Tsuyoshi;Inui, Hiroshi
雄激素受体（AR）是一种配体激活的转录因子，调节参与前列腺发育和肿瘤发生的基因表达。RanBP10与RanBPM具有显著的氨基酸序列相似性，RanBPM是一种众所周知的AR共激活剂。在这里，我们证明了RanBP10增强了AR的配体依赖性转录活性，并与AR形成复合物。RanBP10与RanBPM一起对AR的转激活发挥了加性作用。RanBP10的过表达增强了糖皮质激素受体的转录活性，但对雌激素受体α没有作用。RanBP10在ar阳性前列腺癌LNCaP细胞中高表达，而RanBPM在WI-38和MCF-7细胞中高表达，而在前列腺癌细胞中低表达。RanBP10主要与RanBPM共定位于细胞质和细胞核，并与自身或RanBPM形成蛋白复合物。这些结果表明，RanBP10作为RanBPM的同聚或异聚低聚物增强了AR的活性。(C) 2008爱思唯尔公司版权所有。
Androgen receptor (AR) acts as a ligand-activated transcription factor that regulates the expression of genes involved in prostate development and tumorigenesis. RanBP10 shares significant amino acid sequence similarity with RanBPM that is a well-known AR coactivator. Here, we demonstrate that RanBP10 enhances the ligand-dependent transcriptional activity of AR and forms a complex with AR. RanBP10 together with RanBPM exerted an additive effect on AR transactivation. Overexpression of RanBP10 enhanced transcriptional activity of glucocorticoid receptor, but not estrogen receptor alpha. RanBP10 was highly expressed in AR-positive prostate cancer LNCaP cells, while RanBPM was abundant in WI-38 and MCF-7 cells rather than prostate cancer cells. RanBP10 was mostly co-localized with RanBPM throughout the cytoplasm and nucleus and formed a protein complex with itself or RanBPM. These results suggest that RanBP10 enhances AR transactivation as a homo-oligomer or a hetero-oligomer with RanBPM. (C) 2008 Elsevier Inc. All rights reserved.