...
  • 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Cell cycle >UBE4B, a ubiquitin chain assembly factor, is required for MDM2-mediated p53 polyubiquitination and degradation.
【24h】

UBE4B, a ubiquitin chain assembly factor, is required for MDM2-mediated p53 polyubiquitination and degradation.

机译：MBE2介导的p53多聚泛素化和降解需要UBE4B（泛素链装配因子）。

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

Although MDM2 is known to be a critical negative regulator of p53, MDM2 only catalyzes p53 mono- or multiple monoubiquitination in vitro and in vivo, which is insufficient for the initiation of proteasomal degradation. MDM2 does not polyubiquitinate p53 in vitro, however, which indicates that the activity of other ubiquitin ligase(s) or cofactor(s) is required for MDM2-mediated p53 polyubiquitination and degradation. In our recent study, we demonstrated that UBE4B, an E3 and E4 ubiquitin ligase with a U-box domain, interacts physically with both p53 and MDM2. Our findings revealed that UBE4B negatively regulates the level of p53 and inhibits p53-dependent transactivation and apoptosis. We propose that inhibition of MDM2 binding to UBE4B may provide another approach to inhibit MDM2 E3 ligase activity for tumor suppressor p53. It could lead to novel anticancer therapies, with the possibility of reducing the public health burden from cancer.
机译：尽管已知MDM2是p53的关键负调节剂，但MDM2仅在体外和体内催化p53单泛素化或多重单泛素化，这不足以引发蛋白酶体降解。 MDM2不能在体外多聚泛素化p53，这表明MDM2介导的p53多聚泛素化和降解需要其他泛素连接酶或辅因子的活性。在我们最近的研究中，我们证明了UBE4B（一种具有U-box域的E3和E4泛素连接酶）与p53和MDM2发生物理相互作用。我们的发现表明，UBE4B负调节p53的水平，并抑制p53依赖的反式激活和凋亡。我们提出抑制MDM2与UBE4B的结合可能提供另一种抑制肿瘤抑制因子p53的MDM2 E3连接酶活性的方法。它可能导致新的抗癌治疗，并有可能减轻癌症对公共健康的负担。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 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