Chavez, Melissa
Melissa is a first year trainee and is in the Department of Chemistry and Biochemistry. Her research mentor is Dr. Jorge Torres. She received a B.S. degree in 2009 from UC Irvine.
Mentor: Dr. Jorge Torres
The ubiquitin proteasome pathway plays a critical role in regulating many important biological processes including cell cycle progression. The Cullin family (Cul1-Cul7) of ubiquitin ligases are multi-component enzymes that target proteins for ubiquitination and subsequent degradation by the 26S proteasome. One of the least studied members of the cullin family is Cul7. Cul7 been shown to play a role in the regulation of cell proliferation by interacting with cell cycle regulators like p53, cyclin D, and IRS-1. Cul7 is known to bind to the substrate adaptor FBxW8 but unlike other Cullin proteins, it is not known whether Cul7 can bind to other F-box proteins. We hypothesize that Cul7 can interact and form E3 ligase complexes with other F-box proteins. In order to better understand the physiological role of Cul7 in cell proliferation, we propose to fully examine the interacting proteins of Cul7.
