Application of surface plasmon resonance for analysis of protein-protein interactions in the G protein-mediated signal transduction pathway

Hundreds of extracellular stimuli are received by cells via the pathways co nsisting of three basic components: cell-surface receptors, heterotrimeric G proteins, and intracellular effector enzymes or ion channels. A number of additional molecules, including G protein-coupled receptor kinases (GRKs), phosducin and Ca2+-binding proteins modulate signal transduction through t hese cascades. Understanding how these universal pathways work requires a d etailed analysis of the interactions between these proteins. The recently e merged technology of surface plasmon resonance (SPR) can study protein-prot ein interactions by measuring not only the equilibrium binding constants, b ut also the association and dissociation rates. This article reviews experi mental design used by researchers to analyze different components of the G protein pathway by SPR and focuses on the insights this technique provides regarding the kinetics, structure-function aspects and regulation of specif ic molecular events in the cascade. Copyright (C) 2000 John Whey & Sons, Lt d.