Trafficking and Oligomeric Regulation of Platelet-Activating Factor Acetylhydrolase Type II

Platelet-activating factor acetylhydrolase type II, PAFAH-II, is an intracellular phospholipase A2 enzyme present in various tissues and cells. PAFAH-II hydrolyzes a known phospholipid-derived mediator, platelet-activating factor, as well as oxidatively fragmented phospholipids in cellular membranes. Although the crystal structure of PAFAH-II remains unsolved, homology modeling has provided insight into the components of its structure that are necessary for membrane localization and binding. PAFAH-II contains an N-terminal myristoyl tail as well as two hydrophobic helices that help to control the oligomeric state and the association of the enzyme to membranes. This chapter presents an overview of the experimental methods and results that have developed our current understanding of the trafficking of PAFAH-II to the cellular membranes, as well as the enzyme's natural oligomeric states related to its function.