Complex of PRL3 and CBS-pair domain of CNNM3 (Zhang et al, Sci Rep, 2017)
Conformational change in parkin upon phosphorylation (Sauvé et al, NSMB, 2018)
Our interests are centred on the application of biophysics to the study of protein structure and function.
The laboratory works in two areas: 1) ubiquitination pathways in neurodegenerative diseases and 2) PRLs, a family of highly oncogenic protein phosphatases.
Our structures of parkin, a ubiquitin ligase that protects against Parkinson's disease, showed that parkin is natively inhibited and activated by large conformational change in response to its phosphorylation.
Drugs that increase parkin activity could be used for the treatment of Parkinson's disease. In the second project, we discovered that cysteine phosphorylation regulates the interaction between PRLs and a membrane protein involved in magnesium transport.
To understand how proteins function in these systems, we use multiple biophysical methods: X-ray crystallography, NMR spectroscopy and cryo-electron microscopy.
As part of the McGill Centre for Structural Biology, our equipment includes 600 MHz and 800 MHz NMR spectrometers, a state-of-the-art METALJET X-ray diffraction and scattering system, isothermal titration calorimeters, an analytic ultracentrifuge, crystallization robots and imaging hotels.