Research interests: The Hsp90 chaperoning machinery, the role of the co-chaperone UNC45A (GCUNC45)
Research in Dr. Chadli’s laboratory focuses on understanding and targeting the Hsp90 chaperoning machine for cancer therapy. Molecular chaperones are key players in the maintenance of a healthy proteome and in homeostasis of the cell. Dysregulation in the function of molecular chaperones leads to many metabolic and oncological diseases. Current information suggests that targeting the Hsp90 machine may have a powerful and combinatorial impact on dysfunctional circuitries that underlie cancer. We are developing a novel high-throughput technology to identify impactful chemical compounds to inactivate the core components of the Hsp90 chaperoning machine. We are also dissecting the role of co-chaperones in the initiation and progression of breast and prostate cancers using in vitro and mouse conditional knockout models.
1120 15th Street
Augusta, GA 30912
Office: (706) 721-4661
Chadli A, Felts SJ, Wang Q, Sullivan WP, Botuyan MV, Fauq A, Ramirez-Alvarado M, Mer G. Celastrol inhibits Hsp90 chaperoning of steroid receptors by inducing fibrillization of the Co-chaperone p23. J Biol Chem. 2010 Feb 5;285(6):4224-31.
Chadli A, Felts SJ, Toft DO. GCUNC45 is the first Hsp90 co-chaperone to show alpha / beta isoform specificity. J Biol Chem. 2008 Apr 11;283(15):9509-12.
Chadli A, Bruinsma ES, Stensgard B, Toft D. Analysis of Hsp90 cochaperone interactions reveals a novel mechanism for TPR protein recognition. Biochemistry. 2008 Mar 4;47(9):2850-7.
Publications are updated quarterly. For a complete listing, see Dr. Chaldi's work