Abstract:

Post-translational modification by ubiquitin, catalyzed by the E1-E2-E3 enzyme cascade, regulates diverse cellular processes. This modification primarily occurs between the C-terminus of ubiquitin and ε-amino group of lysine, as well as hydroxyl and thiol groups on proteins. Increasing evidence has revealed the attachment of ubiquitin to non-proteinaceous substrates, including lipids and carbohydrates. Our group has discovered a family of E3 ligases called DELTEX, which share conserved domains that recognize non-proteinaceous substrates such as ADP-ribose and single-stranded nucleic acids and catalyze their ubiquitination. In this talk, I will present these findings.

Bio:

Danny Huang is a Senior Group Leader at the Cancer Research UK Scotland Institute (formerly known as the CRUK Beatson Institute) and holds a professorship at the University of Glasgow. He obtained his PhD in biochemistry and enzymology from the University of Sydney, Australia, in 2002. He then carried out postdoctoral training in Dr. Brenda Schulman’s lab at St. Jude Children’s Research Hospital, where he became interested in understanding the process of ubiquitination and uncovered the structural mechanism of the E1 enzyme. In 2009, he started his independent research group at the Beatson Institute for Cancer Research (now known as CRUK Scotland Institute). The primary goal of his research is to elucidate the mechanisms of ubiquitin ligases and exploit this process for potential cancer therapies. His group has made several key contributions to understanding the mechanisms of ubiquitin ligases (PMID: 22266821, PMID: 22902369, PMID: 23851457, PMID: 25801170, PMID: 29053960, PMID: 32350255, PMID: 32937373, PMID: 32948590, PMID: 35027744, PMID: 39377462).