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Nature Research, Nature Communications, 1(6), 2015

DOI: 10.1038/ncomms6984

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Hydrophobic mismatch sorts SNARE proteins into distinct membrane domains

Journal article published in 2015 by Dragomir Milovanovic ORCID, Alf Honigmann, Seiichi Koike, Fabian Göttfert, Gesa Pähler, Meike Junius, Stefan Müllar, Ulf Diederichsen, Andreas Janshoff, Helmut Grubmüller, Herre J. Risselada, Christian Eggeling, Stefan W. Hell, Geert van den Bogaart ORCID, Geert van den Bogaart and other authors.
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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Abstract

AbstractThe 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.