The separate disciplines of proteomics and lipidomics are now well-established and have evolved independently over the last two decades. In parallel, over the same time period, native mass spectrometry experiments have advanced such that survival of intact protein complexes in the gas phase is now unequivocal. A decade later, with the ability to observe intact membrane protein complexes, it became apparent that these assemblies were often extracted with their associated lipid environments intact. Consequently, it is now possible to study lipids that interact directly with proteins rather than collections of proteins or lipids reported in separate proteomic or lipidomic investigations.
During this lecture I will show how the combination of proteomics and lipidomics is enabling us to identify lipids that are critical to the structure and function of membrane proteins. During our research we have also discovered lipids that modulate associations between membrane proteins, remodel the lipid bilayer in the vicinity of complexes and compete for drug binding sites on receptors. I will use a range of membrane protein assemblies to illustrate these lipid connections including ion channels, transporters, membrane embedded motors and GPCRs.