top of page
Screen Shot 2022-07-01 at 10.40.04 AM.png


Mitochondrial function is dependent on molecular chaperones, primarily due to their necessity in the formation of respiratory complexes and clearance of misfolded proteins. Heat shock proteins (Hsps) are a subset of molecular chaperones that function in all subcellular compartments both constitutively and in response to stress. The Hsp90 chaperone TRAP1 is primarily localized to mitochondria and controls both cellular metabolic reprogramming and mitochondrial apoptosis. TRAP1 upregulation facilitates growth and progression of many cancers by promoting glycolytic metabolism and antagonizing the mitochondrial permeability transition that precedes multiple cell death pathways. TRAP1 attenuation induces apoptosis in cellular models of cancer, identifying TRAP1 as a potential therapeutic target in cancer. Like cytosolic Hsp90 proteins, TRAP1 is also subject to post-translational modifications (PTM) that regulate its function and mediate its impact on downstream effectors, or ‘clients’, however few effectors have been identified to date. 


The goal of my lab is to:

  1. Identify and characterize the bona fide functions of TRAP1 and their impact on cellular metabolic flux

  2. Understand the consequences of TRAP1 de-regulation during oncogenesis and cancer growth 

  3. Assess the impact of post-translational modification on TRAP1 function

Other great work
Truman lab logo V2 2021.png.webp
Screen Shot 2022-07-13 at 10.43.27 AM.png
Mollapour Lab
Truman Lab
Bourboulia Lab
Colombo Lab
van Oosten-Hawle Lab
Hsp90Code-rev7 copy.jpg.webp
The Chaperone Code Club
bottom of page