Biochemical and Biophysical Approaches to Characterize the Molecular Basis of Abnormal Cell Signaling Function Involving Ras-Related Proteins.
Ras proteins are often mutated in several human cancers, making them excellent protein models to probe structure-function relationships of cell-signaling processes mediating cell transformation. Target-based approaches to avert Ras-stimulated abnormal signal transduction should be enhanced by a better understanding of the structural biol. of Ras-related Protein-Protein Interactions (PPIs), as well as, protein function. Cell division cycle 42 (Cdc42) is the model Ras protein being studied by this lab. Mutations as well as PPIs play a significant role in Cdc42-stimulated cell signaling. As such, our goal is to understand key factors, using biophys. and biochem. techniques and approaches, which underlie the mol. basis of Cdc42 activity. Our central hypothesis is that there are unique structural and dynamic features of Cdc42 that can be exploited to modulate protein interactions and influence abnormal cell signaling activity. Recent results in this regard will be presented.