September 2011

Document Type


Degree Name



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



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