...
  • 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Molecular cell >Phosphorylation of NF-κB p65 by PKA Stimulates Transcriptional Activity by Promoting a Novel bivalent Interaction with the Coactivator CBP/p300
【24h】

Phosphorylation of NF-κB p65 by PKA Stimulates Transcriptional Activity by Promoting a Novel bivalent Interaction with the Coactivator CBP/p300

机译：通过PKA磷酸化NF-κBp65，通过促进与共激活剂CBP / p300的新型二价相互作用来刺激转录活性。

获取原文
获取原文并翻译 | 示例
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

The transcriptional activity of NF-κB is stimulated upon phosphorylation of its p65 subunit on serine 276 by protein kinase A (PKA). The transcriptional coactivator CBP/p300 associates with NF-κB p65 through two sites, an N-terminal domain that interacts with the C-terminal region of unphosphorylated p65, and a second domain that only interacts with p65 phosphorylated on serine 276. Accessibility to both sites is blocked in unphosphorylated p65 through an intramolecular masking of the N terminus by the C-terminal region of p65. Phosphorylation by PKA both weakens the interaction between the N- and C-terminal regions of p65 and creates an additional site for interaction with CBP/p300. Therefore, PKA regulates the transcriptional activity of NF-κB by modulating its interaction with CBP/p300.
机译：NF-κB的转录活性通过蛋白激酶A（PKA）在丝氨酸276上的p65亚基磷酸化后得到刺激。转录共激活因子CBP / p300通过两个位点与NF-κBp65缔合，一个N端结构域与未磷酸化p65的C端区域相互作用，第二个域仅与丝氨酸276上磷酸化的p65相互作用。通过p65的C端区域对N端进行分子内掩蔽，可在未磷酸化的p65中封闭这些位点。通过PKA进行的磷酸化作用既削弱了p65的N端和C端之间的相互作用，又创造了一个与CBP / p300相互作用的附加位点。因此，PKA通过调节NF-κB与CBP / p300的相互作用来调节NF-κB的转录活性。

著录项

相似文献

  • 外文文献
  • 专利
获取原文

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号