Understanding the molecular principles that enable chaperonins to maintain protein homeostasis in the cell
Chaperonins are essential molecular machines that safeguard protein homeostasis by assisting nascent and misfolded proteins to achieve their native conformations. Despite their critical role in cellular function, the molecular principles governing how chaperonins recognize diverse substrates, orchestrate the folding process, and prevent aggregation in the crowded cellular environment remain incompletely understood. Our research integrates structural biology, biochemistry, and cell biology to elucidate these problems with mechanistic details and to provide fundamental insights into protein quality control mechanisms with implications for understanding diseases caused by protein misfolding.
Exploring modulation of the tubulin-folding pathway for potential cancer therapy
Chaperonin TRiC guides tubulin maturation, a critical step in microtubule function. As many cancers exploit aberrant microtubule dynamics, we are investigating how modulating TRiC‑mediated tubulin maturation can guide the development of targeted therapies. Integrating structural insights with engineering, we aim to fine‑tune TRiC activity to selectively influence tubulin maturation in tumor cells, with the goal of overcoming resistance to existing agents while minimizing off‑target effects.