Molecular view on protein sorting into liquid-ordered membrane domains mediated by gangliosides and lipid anchors

Djurre H. de Jong; Cesar A. Lopez; Siewert J. Marrink

doi:10.1039/C2FD20086D

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Faraday Discussions

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Molecular view on protein sorting into liquid-ordered membrane domains mediated by gangliosides and lipid anchors

Djurre H. de Jong,^a Cesar A. Lopez^a and Siewert J. Marrink*^a

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Nijenborgh 7, AG Groningen, The Netherlands
E-mail: s.j.marrink@rug.nl ;
Fax: +31 50 363 4398 ;
Tel: +31 50 363 4457

Faraday Discuss., 2013,161, 347-363

DOI: 10.1039/C2FD20086D
Received 27 Apr 2012, Accepted 08 Jun 2012
First published online 11 Jun 2012

This article is part of themed collection: Lipids & Membrane Biophysics

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We present results from coarse grain molecular dynamics simulations of mixed model membranes consisting of saturated and unsaturated lipids together with cholesterol, in which lipid-anchored membrane proteins are embedded. The membrane proteins studied are the peripherally bound H-Ras, N-Ras, and Hedgehog, and the transmembrane peptides WALP and LAT. We provide a molecular view on how the presence and nature of these lipid anchors affects partitioning of the proteins between liquid-ordered and liquid-disordered domains. In addition, we probed the role of the ganglioside lipid GM1 on the protein sorting, showing formation of GM1-protein nano-domains that act as shuttles between the differently ordered membrane regions.

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