- Michael Smith Laboratories
- Department of Biochemistry and Molecular Biology
- Genome Sciences and Technology (GSAT) Graduate Program
- California Institute of Technology, 2002, Postdoctoral Fellow
- University of Geneva and Max Planck Institute of Biochemistry, Germany, 2001, PhD
- University of Geneva, Switzerland, 1997, BSc
Damaged and misfolded proteins that cannot be repaired have to be eliminated from the cell. Failure to do so, leads to the accumulation of these proteins that will then aggregate. Protein aggregation is a hallmark of a large number of neurodegenerative pathologies including Parkinson’s and Prion diseases. The ubiquitin proteasome system pays a major role in targeting aberrant proteins for proteolysis. In this system, target proteins are first modified by the covalent attachment of ubiquitin (i.e., ubiquitylation) and then recognized and degraded by the proteasome. Using a combination of cell biology and proteomic approaches, our lab is interested in understanding how the cell recognizes misfolded proteins to target them for ubiquitylation and proteolysis.
- How is protein homeostasis maintained within the cell?
- How does the cell triage its misfolded proteins?
- Which proteins are potentially more prone to aggregation within the cells upon stress conditions and aging?
Biochemistry, biotechnology, bioinformatics, biological imaging, systems biology, protein regulation, proteomics, synthetic biology, macromolecular biochemistry, regenerative medicine
To learn more about the Mayor Lab, please visit mayorlab.msl.ubc.ca.