Rate My Professor Catherine Day

Her research investigates the molecular basis of signalling, focusing on how ubiquitin regulates protein function, particularly through RING E3 ligases and their mechanisms for ubiquitin chain assembly. Earlier studies explored apoptosis and cell death, including Bcl-2 family protein interactions relevant to cancer. Funding supports her work from the Marsden Fund, Health Research Council of New Zealand, Lottery Health, Genesis Oncology, and the University of Otago. Key publications include 'Zinc finger 1 of the RING E3 ligase, RNF125, interacts with the E2 to enhance ubiquitylation' (Structure, 2023), 'Arkadia and Ark2C promote substrate ubiquitylation with multiple E2 enzymes' (Journal of Molecular Biology, 2025), 'A novel RNF125 variant associated with Tenorio syndrome alters ubiquitin chain binding' (Clinical Genetics, 2024), 'Differential targeting of prosurvival Bcl-2 proteins by their BH3-only ligands allows complementary apoptotic function' (Molecular Cell, 2005), and 'The BH3 mimetic ABT-737 targets selective Bcl-2 proteins and efficiently induces apoptosis via Bak/Bax if Mcl-1 is neutralized' (Cancer Cell, 2006). Professor Day was elected a Fellow of the Royal Society Te Apārangi in 2014 for exceptional distinction in research as an innovative protein biochemist and structural biologist advancing knowledge of protein interactions in cell death and survival. She received the Otago School of Medical Sciences Researcher of the Year award in 2010 and serves as an associate editor for biochemistry and biophysics at Royal Society Open Science.