- 作者: Chang-Tze Ricky Yu; Jiunn-Chyi Wu; Mei-Chih Liao; Shih-Lan Hsu; Chi-Ying F. Huang
- 作者服務機構: 1 Graduate Institute of Biomedicine and Biomedical Technology, National Chi Nan University, Puli, Nantou, 545, Taiwan, R.O.C; ; 2 Department of Education and Research, Taichung Veterans General Hospital, Taichung, 400, Taiwan, R.O.C; ; 3 Institute of Cancer Research, National Health Research Institutes, Taipei, 114, Taiwan, R.O.C; ; 4 Institute of Clinical Medicine, National Yang-Ming University, Taipei, 112, Taiwan, R.O.C; ; 5 Institute of Bio-Pharmaceutical Sciences, National Yang-Ming University, Taipei, 112, Taiwan, R.O.C; ; 6 Institute of Biotechnology in Medicine, National Yang-Ming University, Taipei, 112, Taiwan, R.O.C
- 中文摘要: --
- 英文摘要: The c-Fos has been implicated in the regulation of gene expression under a variety of stimuli. It is known that c-Fos undergoes protein phosphorylation, which may subsequently modulate diverse functions in cells. However, less is known about the role and phosphorylation status of c-Fos during mitosis. Here, we showed that c-Fos exhibited an electrophoretic mobility up-shift as detected by SDS-PAGE during mitosis, which is an indication of protein phosphorylation. Aurora-Α, but not Aurora-B or -C, serves as one of the kinases catalyzing the mitotic phosphorylation of c-Fos. The mobility up-shift was partially abolished by introducing siRNA or a catalytically inactive form of Aurora-Α. Moreover, ectopic expression of the wild type, but not the catalytically inactive form of Aurora-A resulted in the alteration of c-Fos complex formation, suggesting Aurora-A is engaged in the regulation of c-Fos protein-protein interaction. These findings imply that c-Fos may undergo cell cycle dependent phosphorylation, in which some kinases including Aurora-A play a role in catalyzing the post translational modification of c-Fos.
- 中文關鍵字: --
- 英文關鍵字: c-Fos, Aurora-Α, Mitotic phosphorylation