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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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Identifier
  • 64371
  • E-project-042722-135141
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  • 2022
Date created
  • 2022-04-27
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