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Proc Natl Acad Sci U S A. 2011 Jan 25;108(4):1343-8. doi: 10.1073/pnas.1009362108. Epub 2011 Jan 4.

Lipid packing drives the segregation of transmembrane helices into disordered lipid domains in model membranes.

Author information

1
Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 7, 9747 AG Groningen, The Netherlands. l.schafer@rug.nl

Abstract

Cell membranes are comprised of multicomponent lipid and protein mixtures that exhibit a complex partitioning behavior. Regions of structural and compositional heterogeneity play a major role in the sorting and self-assembly of proteins, and their clustering into higher-order oligomers. Here, we use computer simulations and optical microscopy to study the sorting of transmembrane helices into the liquid-disordered domains of phase-separated model membranes, irrespective of peptide-lipid hydrophobic mismatch. Free energy calculations show that the enthalpic contribution due to the packing of the lipids drives the lateral sorting of the helices. Hydrophobic mismatch regulates the clustering into either small dynamic or large static aggregates. These results reveal important molecular driving forces for the lateral organization and self-assembly of transmembrane helices in heterogeneous model membranes, with implications for the formation of functional protein complexes in real cells.

PMID:
21205902
PMCID:
PMC3029762
DOI:
10.1073/pnas.1009362108
[Indexed for MEDLINE]
Free PMC Article

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