Our research focuses on understanding how proteins are targeted by the ubiquitin-proteasome system (UPS)and how aberration of this system contributes to pathogenesis of diseases. Ubiquitination is a post-translational modification in which ubiquitin is covalently attached onto a substrate protein to alter the function and fate of the protein within the cell. It is a highly dynamic and regulatory process that governs nearly every fundamental cellular process, from cell cycle control, cell signaling, and stress response to regulation of protein stability and turnover. As such, deregulation of protein ubiquitination leads to a vast array of human diseases including cancers, immune disorders and neurodegenerative diseases. Understanding the mechanism and regulation of protein ubiquitination is therefore essential for elucidating the role of UPS in pathogenesis of these diseases and for the development of new strategies and therapeutics.
Molecular Biology and Biochemistry, Structural Biology