How curved membranes recruit amphipathic helices and protein anchoring motifs

Research output: Contribution to journalJournal articleResearchpeer-review

Nikos Hatzakis, Vikram Kjøller Bhatia, Jannik Larsen, Kenneth Lindegaard Madsen, Pierre-Yves Bolinger, Andreas Hjarne Kunding, John Jairo Castillo Leon, Ulrik Gether, Per Hedegård, Dimitrios Stamou

Lipids and several specialized proteins are thought to be able to sense the curvature of membranes (MC). Here we used quantitative fluorescence microscopy to measure curvature-selective binding of amphipathic motifs on single liposomes 50-700 nm in diameter. Our results revealed that sensing is predominantly mediated by a higher density of binding sites on curved membranes instead of higher affinity. We proposed a model based on curvature-induced defects in lipid packing that related these findings to lipid sorting and accurately predicted the existence of a new ubiquitous class of curvature sensors: membrane-anchored proteins. The fact that unrelated structural motifs such as alpha-helices and alkyl chains sense MC led us to propose that MC sensing is a generic property of curved membranes rather than a property of the anchoring molecules. We therefore anticipate that MC will promote the redistribution of proteins that are anchored in membranes through other types of hydrophobic moieties.
Original languageEnglish
JournalNature Chemical Biology
Volume5
Issue number11
Pages (from-to)835-841
Number of pages6
ISSN1552-4450
DOIs
Publication statusPublished - 2009

Bibliographical note

Keywords: Biotinylation; Fluoresceins; Kinetics; Lipid Bilayers; Liposomes; Membrane Lipids; Membrane Proteins; Membranes; Microscopy, Confocal; Microscopy, Fluorescence; Models, Molecular; Peptides

ID: 21593748