Mark Woodford, PhD
Molecular chaperones, TRAP1, Renal cell carcinoma, Metabolic flux, Mitochondrial Function, Post-translational modification
ASSOCIATIONS / MEMBERSHIPS
Heat shock protein-90 (Hsp90) is a molecular chaperone involved in the folding, stabilization, and activation of hundreds of cellular proteins. TRAP1 is the dedicated mitochondrial isoform of Hsp90 and participates in the regulation of metabolic flux, calcium homeostasis, and mitochondrial apoptosis. TRAP1 is upregulated in many cancers, and isoform-specific TRAP1 inhibitors have shown anti-cancer activity in pre-clinical evaluation. Post-translational modification (PTM) is an important regulatory mechanism for Hsp90 molecular chaperones, however little is known about the post-translational landscape of TRAP1. Our lab works to understand the role of TRAP1 activity in mediating tumorigenesis and the impact of PTM on the biological role of TRAP1 in our cellular models of kidney, prostate, and bladder cancer.