Degradation of the nucleotide GDP from the ras protein Cdc42 wild type

by Russell, Erika; Adams, Paul D.

The research focused on studying, at the mol. level, protein structure and function in Ras protein Cdc42 and its involvement in abnormal cell regulation signals that leads to oncogenesis. The specific purpose of the research was to examine possible new ways to liberate GDP from the protein of interest Cdc42Hs. Two expts. were tried to try to create apo-Cdc42Hs. First, the fluorescent analog of GDP was degraded using Alk. Phosphatase. Secondly, Cibracon Blue was used as possible affinity matrix due to its high affinity for ADP-binding proteins and because it binds to ADP it should also bind to GDP. Alk. Phosphatase successfully degraded the fluorescent analog of Cdc42 wt. Which gives reason to believe that it would do the same in Cdc42Hs. With apo-Cdc42Hs there will be a better understanding of the structure of Cdc42Hs. Which could potentially reveal insights on GDP dissocns. and how this leads to cell proliferation.