研究方向
泛素化系统在NF-κB信号转导中以及哺乳动物胚胎干细胞和配子发生中的作用.
Biochemical regulation of NF-κB, embryonic stem cells and gamete biogenesis by the ubiquitination system
In cells, many proteins undergo post-translational modifications under certain physiological as well as pathological conditions. As many as 300 post-translational modifications of proteins are known to occur in cells: phosphorylation, acetylation, methylation, ubiquitination and so on.
Ubiquitin is a small protein of only 76 amino acids in length that is ubiquitously expressed in all cells and is highly conserved from yeast to human. Modification of proteins by ubiquitin is achieved through the process called ubiquitination in which the carboxyl group of the last glycine residue at the C-terminus of ubiquitin is covalently attached to the ε-amino group of a lysine residue on the target protein resulting in the formation of an isopeptide bond. The ubiquitination process is a coordinated three-step enzymatic reaction (Figure 1). In human genome it encodes more than 40 E2s and 500 E3s.
Ubiquitination is rich in information and regulates a variety of cellular processes including but not limited to protein degradation, endocytosis and intracellular protein trafficking, kinase activation and DNA repair. The importance of the ubiquitination system is comparable to that of kinases. Studies on the ubiquitination system and its regulation on other cellular processes are becoming the forefront of biomedical research.