We are interested in questions related to membrane protein biogenesis structure and function. Membrane proteins represent a significant portion of the proteome (20-30%) and they mediate numerous processes essential to life. As such, membrane proteins are linked to many human disorders and often utilized as drug targets.

Biosynthetically, structurally and functionally, membrane proteins follow principles that are different from those of globular proteins. For example, unlike soluble proteins, most membrane proteins must be translated by membrane bound ribosomes; they fold into active enzymes through mechanisms that are only vaguely understood; their structures are dramatically influenced by the necessity to cross the membrane in a zig-zag fashion; their proper function is often regulated by bound lipids; and they undergo recycling by mechanistically fascinating degradation pathways.

Our laboratory has several ongoing membrane protein-related research projects. (i) We investigate the mechanism underlying secondary multidrug (Mdr) efflux. (ii) We study, in live cells, the biosynthetic pathway of membrane proteins. And (iii) we implement the knowledge obtained in project (ii) to facilitate better expression of membrane proteins for biochemical and structural studies. The investigated model membrane proteins belong to the rhomboid family of intramembrane serine proteases.