source: Milwaukee School of Engineering Center for BioMolecular Modeling

year: 2010

authors: Nathan Hale High School SMART Team: Sara Baker, Chelsea Fujinaka, Melissa Gall, Laenzio Garrett, Nick Goldner, Zach Koepp, Valerie Lamphear, Peter Nguyen, Vivek Patel, Stefan Pietrzak, Evan Rypel, Ajay Sreekanth, Kyle Tretow, Tyler Zajdel

Poster Presentation

Abstract: Colorectal cancer affects 1 in 18 Americans, and is linked to mutations in the Adenomatous Polyposis Coli (APC) gene. The rapid division of colonocytes is regulated by the Wingless Type (Wnt) signaling pathway, mediated by β-catenin. In the nucleus, β- catenin binds to Transcription Cell Factor (TCF) and initiates transcription of cell cycle proteins. Alternatively, β-catenin binds to the 20-amino acid repeat region of the APC protein with the help of the scaffold axin. The enzyme GSK-3 then phosphorylates threonine and serine residues of the APC protein and subsequently β -catenin. Phosphorylated β -catenin is degraded, slowing mitosis. Mutations in APC allow β-catenin to accumulate, resulting in hyperproliferation of colonocytes, an early step in colon cancer development. As such, better understanding of APC and its function could potentially lead to better diagnosis and treatment in colorectal cancer.