Abstract
Membrane traffic requires membrane deformation to generate vesicles and tubules. Strong evidence suggests that assembly of curvature-active proteins can drive such membrane shape changes. Well-documented pathways often involve protein scaffolds, in particular coats (clathrin or COP). However, membrane curvature should, in principle, be influenced by any protein binding asymmetrically on a membrane; large membrane morphological changes could result from their aggregation. In the case of Shiga toxin or viral matrix proteins, tubules and buds appear to result from the cargo-driven formation of protein-lipid nanodomains, showing that collective protein behaviour is crucial in the process. We argue here that a combination of in vitro experiments on giant unilamellar vesicles and theoretical modelling based on statistical physics is ideally suited to tackle these collective effects.
Published Version
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