TRAFFICKING THROMBIN RECEPTORS - BIODIVERSITY ON THE RECEPTOR SUPERHIGHWAY

In the past several years, the identification of the human thrombin receptor has permitted considerable progress to be made in the understanding of the ways in which thrombin activates cells. To date, only a single receptor for thrombin has been identified: a member of the G protein-coupled family of receptors that has proved to be a proteolytic substrate for thrombin. Cleavage of the receptor enables it to activate, but also leaves it in a state in which it is unable to respond to thrombin a second time. This review examines the variety of cellular response mechanisms to thrombin, and the growing evidence for diversity among cells in the processes that remove and replace cleaved thrombin receptors, issues that are central to the development of therapeutically useful thrombin receptor antagonists.