Membrane protein sorting and clustering

Cell membranes are comprised of a heterogeneous mixture of lipids and proteins. The heterogeneity of biological membranes plays an important role in cellular function. Despite experimental progress in recent years, the characterization of lateral organization in biological membranes, however, remains challenging due to the lack of tools to study fluctuating nanoscale assemblies in living cells.

The MD group uses large scale simulations to probe the lateral partitioning and self-assembly of proteins. Together with our experimental collaborator Bert Poolman, we aim to unravel the lipid-mediated driving forces underlying protein sorting and clustering, and predict physical mechanisms that could be relevant in real cells.

[1] L.V. Schafer, D.H. de Jong, A. Holt, A.J. Rzepiela, A.H. de Vries, B. Poolman, J.A. Killian, S.J. Marrink. Lipid packing drives the segregation of transmembrane helices into disordered lipid domains in model biomembranes. PNAS, 108:1343-1348, 2011
[2] J. Domanski, S.J. Marrink, L.V. Schaefer. Transmembrane helices can induce domain formation in crowded model biomembranes. BBA Biomembr., 1818:984-994, 2012
[3] D.H. de Jong, C.A. Lopez, S.J. Marrink. Molecular view on protein sorting into liquid-ordered membrane domains mediated by gangliosides and lipid anchors. Farad. Discuss., 161:347-363, 2013.
[4] S. Ramadurai, A. Holt, L.V. Schäfer, V.V. Krasnikov, D.T.S. Rijkers, S.J. Marrink, J.A. Killian, B. Poolman. Influence of hydrophobic mismatch and amino acid composition on the lateral diffusion of transmembrane peptides. Biophys. J.,99:1447-1454, 2010