How curved membranes recruit amphipathic helices and protein anchoring motifs
Research output: Contribution to journal › Journal article › Research › peer-review
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 language | English |
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Journal | Nature Chemical Biology |
Volume | 5 |
Issue number | 11 |
Pages (from-to) | 835-841 |
Number of pages | 6 |
ISSN | 1552-4450 |
DOIs | |
Publication status | Published - 2009 |
Bibliographical note
Keywords: Biotinylation; Fluoresceins; Kinetics; Lipid Bilayers; Liposomes; Membrane Lipids; Membrane Proteins; Membranes; Microscopy, Confocal; Microscopy, Fluorescence; Models, Molecular; Peptides
ID: 21593748