Investigating Kek1 Inhibition of dEGFR

Doherty, Sarah

Student Work

Investigating Kek1 Inhibition of dEGFR

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The Epidermal Growth Factor Receptor (EGFR) family of tyrosine kinases plays a key role in cancer. In humans, the EGFR receptors are organized into four extracellular domains, while in Drosophila the receptor has a fifth domain (V). Kekkon1, a novel inhibitor of dEGFR, does not bind the human receptors due to the binding specificity of Domain V. However, addition of Domain V to human ErbB2 does not impart binding. Our model suggested a loop protruding from Domain IV in humans sterically blocks Kek1 access to Domain V in chimeras. To better understand Kek1 inhibition of dEGFR, a series of ErbB2/dEGFR chimeras were expressed to further investigate Domain IV. A phylogenetic analysis was also conducted to investigate evolution of Domain V mediated regulation. Through these studies, we hope to gain insight into the regulation of the ErbB family that may lead to new therapeutic avenues.

This report represents the work of one or more WPI undergraduate students submitted to the faculty as evidence of completion of a degree requirement. WPI routinely publishes these reports on its website without editorial or peer review.

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