Rate My Professor William Fuller

Fuller’s laboratory investigates the organisation and regulation of cardiac membrane proteins and microdomains in health and disease, using subcellular fractionation, imaging, affinity purification, biochemical, cell, and organ physiological techniques. The research elucidates molecular physiology of membrane proteins, ion transporters, and regulators to understand physiological control of cardiac function and develop therapeutic strategies for cardiovascular diseases. Current projects encompass regulation of transmembrane sodium transport by post-translational phosphorylation and palmitoylation of ion transporters, channels, and regulators; palmitoylation of the ventricular sodium-calcium exchanger NCX1 and L-type Ca channel Cav1.2; palmitoylation regulation of cardiac voltage-sensitive potassium channels and NADPH oxidase superoxide production; substrate recognition and regulation of zDHHC palmitoyl acyl transferase enzymes; PROTAC-mediated targeted degradation of zDHHC enzymes in collaboration with the School of Chemistry; and phospholamban as a therapeutic target for heart failure. Key publications include 'Nanobody-thioesterase chimeras to specifically target protein palmitoylation' (Nature Communications, 2025), 'Elevated Na+ is a dynamic and reversible modulator of mitochondrial metabolism in the heart' (Nature Communications, 2024), 'Palmitoylation of the pore-forming subunit of Cav1.2 controls channel voltage sensitivity and calcium transients in cardiac myocytes' (PNAS, 2023), 'Glutathione-dependent depalmitoylation of phospholemman by peroxiredoxin 6' (Cell Reports, 2024), and highly cited earlier works such as 'Substrate recognition by the cell surface palmitoyl transferase DHHC5' (PNAS, 2014) and 'Off-target effects of sodium-glucose co-transporter 2 blockers: empagliflozin does not inhibit Na+/H+ exchanger-1' (Cardiovascular Research, 2021). Fuller serves on the Editorial Board of Cardiovascular Research and was a guest editor for Frontiers in Physiology.