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Hydrophobic mismatch sorts SNARE proteins into distinct membrane domains

Milovanovic, Dragomir, Honigmann, Alf, Koike, Seiichi, Göttfert, Fabian, Pähler, Gesa, Junius, Meike, Müllar, Stefan, Diederichsen, Ulf, Janshoff, Andreas, Grubmüller, Helmut, Risselada, Herre J., Eggeling, Christian, Hell, Stefan W., van den Bogaart, Geert, Jahn, Reinhard·2015·Nature Communications
DOI 10.1038/ncomms6984PMC PMC4313621
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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.

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Metadata

Authors
Milovanovic, D., Honigmann, A., Koike, S., Göttfert, F., Pähler, G., Junius, M., Müllar, S., Diederichsen, U., Janshoff, A., Grubmüller, H., Risselada, H. J., Eggeling, C., Hell, S. W., van den Bogaart, G., & Jahn, R.
Venue
Nature Communications
Publisher
Springer Science and Business Media LLC
Published
2015-01-30
Volume
6
Issue
1
ISSN
2041-1723
DOI
10.1038/ncomms6984
PMC
PMC4313621
Cited by
162
References
2
Language
en
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