I have studied stress signalling and proteostasis throughout my PhD and postdoctoral training, and am building on this expertise in my own group at The Babraham Institute.

After my undergraduate studies in Natural Sciences (Part II Biochemistry) at University of Cambridge (2004–2007), I did my PhD in Paul Workman’s group at The Institute of Cancer Research (2007–2012), where I investigated the role of ubiquitylation machineries in the degradation of oncogenic protein kinases upon inhibition of the molecular chaperone HSP90. Following a short postdoc carrying on this work alongside an industrial drug-discovery collaboration with Merck-Serono, I moved to California in 2014 to start a postdoc in Judith Frydman’s lab (Stanford University). Here, I used the model organism Saccharomyces cerevisiae (budding yeast) to expand understanding of the molecular circuits involved in misfolded protein clearance, and how these vary depending on their sub-cellular localisation.

I started as a Tenure-track Group Leader at Babraham Institute in 2019. Our group uses a combination of mass spectrometry–based proteomics, live-cell imaging, and bespoke biochemical tools, to tease apart how communication between protein clearance systems contribute to healthy proteostasis, and how this goes awry during ageing and associated stresses. Much of the group currently focuses on the interplay between loss of proteostasis and cellular senescence as two hallmarks of ageing.