Pathogenic mutations in these receptors disrupt normal receptor activity and are known to be responsible for a wide spectrum of abnormalities and illnesses, from dwarfism to bladder cancer.
“Numerous tyrosine kinase inhibitors are on the market as drugs targeting activity of FGF receptors but such drugs have not shown great success,” says Dr. Sarvenaz Sarabipour, a postdoctoral researcher at Johns Hopkins University. “This is largely due to the fact that the mechanism of action of the receptors remains unknown and attempts across many fields to unravel the receptor-ligand specificity have revealed little information.”
FGF receptors, like other cell surface receptors, sense extracellular clues or growth factors and generate distinct signals, initiating cascades of protein-protein interactions inside a cell. The transmitted signals control all aspects of cell fate and are central to the formation of malignant cells.
Sarabipour—in collaboration with Dr. Kalina Hristova, Marlin U. Zimmerman Jr. Faculty Scholar and professor of materials science and engineering at Johns Hopkins University—has found a direct, significant correlation between structure and activation for FGF receptors in response to FGF ligands. Their findings have been reported in the January 2016 issue of Nature Communications. Excerpted from the Materials Science & Engineering website.