ABSTRACT
Specific protein-protein interactions underlie many fundamental cellular processes, such as gene transcription, mRNA splicing, and signal transduction. Many biochemical, genetic, and molecular biological techniques have provided the opportunity for investigators to identify specific protein interactions. This chapter focuses on the application of the yeast two-hybrid genetic screen in the isolation of a novel protein serine/threonine kinase, ILK, mediating integrin signal transduction. The two-hybrid strategy exploits the modularity of protein structure, particularly the independent action displayed by DNA-binding and transactivating domains of transcription factors. Crucial to the success of an interaction trap experiment is the nature of the bait construct used to program the screen.
