The role of hHR23A in mammalian cells migration and invasion

• Main Authors: Shao-Yi Tang, 唐紹溢
• Other Authors: 莊秀美
• Format: Others
• Language: en_US
• Published: 2014
• Online Access: http://ndltd.ncl.edu.tw/handle/60478244281368199212

碩士 === 國立中興大學 === 生物醫學研究所 === 102 === Rad23 is an approximately 400 amino acids protein and evolutionarily conserved from yeast to human. Yeast Rad23 and mammalian homologs, hHR23A and hHR23B are originally identified as an important factor involved in DNA repair and targeting ubiquitinated proteins for 26S protein degradation. The Ubiquitin-Proteasome System(UPS) is responsible for protein quality control. Ubiquitin is activated by Ubiquitin-activating enzyme (E1) and transfers to Ubiquitin-conjugating enzyme (E2),the Ubiquitin-ligase (E3) will replace ubiquitin from E2 to target protein and form a polyubiquitin chain. It has been found that hHR23 contains multiple functions. Here, we found knockdown of hHR23A makes the cell morphology change and increases the expression of Twist1. Twist1 is a transcription factor that promotes epithelial–mesenchymal transition (EMT). By immuonprecipitation, we found hHR23A interacts with Twist1 and regulates Twist1 protein stability. In addition, we found that depletion of hHR23A caused cell migration and metastasis. Taken together, we showed that hHR23A may have a role to regulate migration, even metastasis.