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Hydrophobic mismatch sorts SNARE proteins into distinct membrane domains

Dragomir Milovanovic,A. Honigmann,Seiichi Koike,F. Göttfert,Gesa Pähler,Meike Junius,S. Müllar,U. Diederichsen,A. Janshoff,H. Grubmüller,H. Risselada,C. Eggeling,S. Hell,Geert van den Bogaart,R. Jahn

Published 2015 in Nature Communications

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. Clustering of proteins in the plasma membrane plays an important role in the regulation of both cellular signalling and membrane remodelling. Milovanovic et al.demonstrate that mismatch between transmembrane domain length and the lipid bilayer thickness is sufficient to drive clustering of SNARE proteins.

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