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Nat Commun. 2015 Jan 30;6:5984. doi: 10.1038/ncomms6984.

Hydrophobic mismatch sorts SNARE proteins into distinct membrane domains.

Author information

1
Department of Neurobiology, Max Planck Institute for Biophysical Chemistry, D-37077 Göttingen, Germany.
2
Department of NanoBiophotonics, Max Planck Institute for Biophysical Chemistry, D-37077 Göttingen, Germany.
3
Institute for Physical Chemistry, Georg-August-University, Göttingen D-37077, Germany.
4
Institute for Organic and Biomolecular Chemistry, Georg-August-University, Göttingen D-37077, Germany.
5
Department of Theoretical and Computational Biophysics, Max Planck Institute for Biophysical Chemistry, D-37077 Göttingen, Germany.
6
1] Department of Theoretical and Computational Biophysics, Max Planck Institute for Biophysical Chemistry, D-37077 Göttingen, Germany [2] Department of Chemistry, Leibnitz Institute of Surface Modification, D-04318 Leipzig, Germany.
7
1] Department of NanoBiophotonics, Max Planck Institute for Biophysical Chemistry, D-37077 Göttingen, Germany [2] MRC Human Immunology Unit, Weatherall Institute of Molecular Medicine, University of Oxford, Oxford OX3 9DS, UK.
8
1] Department of Neurobiology, Max Planck Institute for Biophysical Chemistry, D-37077 Göttingen, Germany [2] Department of Tumor Immunology, Radboud University Medical Center, 6525 GA Nijmegen, The Netherlands.

Abstract

The clustering of proteins and lipids in distinct microdomains is emerging as an important principle for the spatial patterning of biological membranes. Such domain formation can be the result of hydrophobic and ionic interactions with membrane lipids as well as of specific protein-protein interactions. Here using plasma membrane-resident SNARE proteins as model, we show that hydrophobic mismatch between the length of transmembrane domains (TMDs) and the thickness of the lipid membrane suffices to induce clustering of proteins. Even when the TMDs differ in length by only a single residue, hydrophobic mismatch can segregate structurally closely homologous membrane proteins in distinct membrane domains. Domain formation is further fine-tuned by interactions with polyanionic phosphoinositides and homo and heterotypic protein interactions. Our findings demonstrate that hydrophobic mismatch contributes to the structural organization of membranes.

PMID:
25635869
PMCID:
PMC4313621
DOI:
10.1038/ncomms6984
[Indexed for MEDLINE]
Free PMC Article

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