The general objective of our team is to investigate at the molecular level the function and regulation of the ubiquitin system.
Ubiquitin is a protein conserved in all eukaryotes that gets conjugated to other proteins in a process termed ubiquitylation. It encodes diverse molecular signals that control the activity and degradation of a very wide array of cellular proteins. Ubiquitylation defects lead to unbalances in the cellular protein content and are associated with numerous human pathologies, including cancers and neurodegenerative diseases.
The fundamental principles governing ubiquitylation are now understood; however we are far from knowing its full functional spectrum. For instance, many of the ubiquitylation and deubiquitylation enzymes that attach and remove ubiquitin to and from cellular proteins are not comprehensively studied and their specific substrates and functions are often partly described, if at all. Our main objectives are to further characterize the general principles that govern ubiquitylation and to identify new cellular pathways regulated by ubiquitylation. To this end, we are using budding yeast (S. cerevisiae) as a model organism and a combination of system wide genetic, live cell imaging and biochemical approaches as well as bioinformatics to analyse our data. We are also collaborating with medicinal chemists to identify small molecule compounds that target the ubiquitin system for research or therapeutic use.