Structural properties of model phosphatidylcholine flippases

Marcella Langer, Rashmi Sah, Anika Veser, Markus Gütlich, Dieter Langosch

Research output: Contribution to journalArticlepeer-review

19 Scopus citations

Abstract

Lipid translocation from one lipid bilayer leaflet to the other, termed flip-flop, is required for the distribution of newly synthesized phospholipids during membrane biogenesis. However, a dedicated biogenic lipid flippase has not yet been identified. Here, we show that the efficiency by which model transmembrane peptides facilitate flip of reporter lipids with different headgroups critically depends on their content of helix-destabilizing residues, the charge state of polar flanking residues, and the composition of the host membrane. In particular, increased backbone dynamics of the transmembrane helix relates to its increased ability to flip lipids with phosphatidylcholine and phosphatidylserine headgroups, whereas a more rigid helix favors phosphatidylethanolamine flip. Further, the transmembrane domains of many SNARE protein subtypes share essential features with the dynamic model peptides. Indeed, recombinant SNAREs possess significant lipid flippase activity.

Original languageEnglish
Pages (from-to)63-72
Number of pages10
JournalChemistry and Biology
Volume20
Issue number1
DOIs
StatePublished - 24 Jan 2013

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