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Journal Article

Hydrophobic mismatch sorts SNARE proteins into distinct membrane domains.

MPS-Authors
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Milovanovic,  D.
Department of NanoBiophotonics, MPI for biophysical chemistry, Max Planck Society;

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Honigmann,  A.
Department of NanoBiophotonics, MPI for biophysical chemistry, Max Planck Society;

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Göttfert,  F.
Department of NanoBiophotonics, MPI for biophysical chemistry, Max Planck Society;

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Grubmüller,  H.
Department of Theoretical and Computational Biophysics, MPI for biophysical chemistry, Max Planck Society;

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Risselada,  H. J.
Department of Theoretical and Computational Biophysics, MPI for biophysical chemistry, Max Planck Society;

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Eggeling,  C.
Department of NanoBiophotonics, MPI for biophysical chemistry, Max Planck Society;

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Hell,  S. W.
Department of NanoBiophotonics, MPI for biophysical chemistry, Max Planck Society;

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van den Bogaart,  G.
Department of Neurobiology, MPI for biophysical chemistry, Max Planck Society;

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Jahn,  R.
Department of Neurobiology, MPI for biophysical chemistry, Max Planck Society;

Fulltext (public)

2111472.pdf
(Publisher version), 1002KB

Supplementary Material (public)

2111472_Suppl.pdf
(Supplementary material), 887KB

Citation

Milovanovic, D., Honigmann, A., Koike, S., Göttfert, F., Pahler, G., Junius, M., et al. (2015). Hydrophobic mismatch sorts SNARE proteins into distinct membrane domains. Nature Communications, 6: 5984. doi:10.1038/ncomms6984.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0025-6C39-A
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.