My research interests centre on understanding the intracellular protein degradation mechanisms used by eukaryotic cells to stay healthy and respond to various stresses. These comprise autophagy and the ubiquitin-proteasome system.

Autophagy is a 'self-eating' process whereby cells digest their own contents through formation of a new double-membraned organelle called an autophagosome. These organelles later fuse with degradative lysosomes. I first became interested in autophagy during my PhD and first postdoc at UCL Laboratory for Molecular Cell Biology in Prof Robin Ketteler's lab. During this time, I dissected the role of the ATG4 proteases in human cells. I used CRISPR/Cas9 genome editing to disrupt the different human ATG4(A-D) isoforms, and studied the effects on autophagy using biochemical methods as well as confocal and electron microscopy.

My second postdoc exposed me to yeast genetics and state-of-the art molecular techniques including proteomics and phosphorylation analysis. This was based in Dr Adrien Rousseau's lab at MRC Protein Phosphorylation and Ubiquitylation Unit (PPU), University of Dundee. I studied the proteasome, an essential large multiprotein complex responsible for degrading most proteins in the cell. In this project I helped identify multiple stress-sensitive phosphorylation sites on a protein (Shp1/p47) linked closely to proteasome function.

My current lecturing position in UCL Cell & Developmental Biology (CDB) is focused on teaching, but I retain a keen interest in protein degradation mechanisms. I am working closely with Prof Sandip Patel's lab as an 'honorary member' to start developing my own independent research and explore the link between autophagy and TPC (two-pore channel) proteins found on endolysosome membranes. In the near future, I hope to be able to provide training and supervision to new students, and in doing so, help clarify the mysterious role of calcium ions in the regulation of autophagy.