Dept. of Cell and Developmental Biology
Oregon Health & Science University
Fibroblast growth factor receptor 3 (FGFR3) is an important regulator of growth and differentiation, whose aberrant activation by mutation causes a number of genetic diseases including skeletal diseases and cancer. I found that FGFR3 strongly associates with Hsp90 chaperone complexes. Hsp90 function has become a drug target for several diseases because it can be modulated using small molecule inhibitors to alter the stability of disease-causing proteins. This dissertation details the experiments characterizing the role of Hsp90 chaperone complexes in FGFR3 and FGFR family stability, and examines the use of Hsp90 inhibitors in pre-clinical models of FGFR3-mediated disease. Chapter 1 outlines the background on FGFR3 and its role in disease, the function of Hsp90 chaperone complexes and the use of small molecule inhibitors of Hsp90. Chapter 2 summarizes data characterizing the role of Hsp90 chaperone complexes in the stability of FGFR3 and the FGFR family. This chapter documents that FG
School of Medicine
Laederich, Melanie B., "Defining the role of HSP90 in the stability of FGFR3 and as a drug target for the treatment of skeletal diseases and cancer" (2011). Scholar Archive. 621.