REGγ modulates p53 activity by regulating its cellular localization

• DOI: 10.1242/jcs.067405
• Publication Date: 2010-11-17T18:16:26Z
• Authors: Jian Liu; Guowu Yu; Yanyan Zhao; Dengpan Zhao; Ying Wang; Lu Wang; Jiang Liu; Lei Li; Yu Zeng; Yongyan Dang; Chuangui Wang; Guang Gao; Weiwen Long; David M. Lonard; Shanlou Qiao; Ming-Jer Tsai; Bianhong Zhang; Honglin Luo; Xiaotao Li
• Keywords: Nuclear export signal

The proteasome activator REGγ mediates a shortcut for the destruction of intact mammalian proteins. biological roles and underlying mechanisms are not fully understood. Here we provide evidence that regulates cellular distribution p53 by facilitating its multiple monoubiquitylation subsequent nuclear export degradation. We also show inhibition tetramerization might further enhance cytoplasmic relocation reduce active in nucleus. Furthermore, enhances physical interaction with HDM2 probably facilitates polyubiquitylation p53, suggesting can act as signal Depletion sensitizes cells to stress-induced apoptosis, validating crucial role control through regulation function. Using mouse xenograft model, knockdown results significant reduction tumor growth, an important development. Our study therefore demonstrates REGγ-mediated inactivation is one involved cancer progression.