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Transbilayer movement of lipids

Glycolipid transport (flipping) from the cytoplasmic to the luminal side of the endoplasmic reticulum represents an essential step during the assembly of the oligosaccharide donor for N-glycosylation of proteins. So far genetic and biochemical experiments have failed to identify the flippase(s) mediating this process. However, experimental evidence form several laboratories, including our own, suggests the involvement of the endoplasmic reticulum protein, Rft1, in this process. Using T. brucei as model organism, our current work aims to elucidate Rft1's function by identifying its interaction partners and its role in glycolipid transport.

We are also studying the mechanisms involved in lipid transport across phospholipid bilayers. The mechanism of ATP-independent lipid flip-flop across biomembranes is not known in any system, but a common hypothesis is that lipid transport proteins are required. Recently, Menon and co-workers (Curr Biol 21: 149, 2011; Nat Commun 5: 5115, 2014) demonstrated that rhodopsin, in addition to its well-known function in visual transduction, acts as ATP-independent phospholipid flippase. We are currently setting up assays to study rhodopsin-mediated phospholipid flipping using natural phospholipids as substrates, to extend previous studies in which synthetic lipid probes have been used.

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