Hydrophobic mismatch sorts SNARE proteins into distinct membrane domains

Dragomir Milovanovic, 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 () and Reinhard Jahn ()
Additional contact information
Dragomir Milovanovic: Max Planck Institute for Biophysical Chemistry
Alf Honigmann: Max Planck Institute for Biophysical Chemistry
Seiichi Koike: Max Planck Institute for Biophysical Chemistry
Fabian Göttfert: Max Planck Institute for Biophysical Chemistry
Gesa Pähler: Institute for Physical Chemistry, Georg-August-University
Meike Junius: Institute for Organic and Biomolecular Chemistry, Georg-August-University
Stefan Müllar: Institute for Organic and Biomolecular Chemistry, Georg-August-University
Ulf Diederichsen: Institute for Organic and Biomolecular Chemistry, Georg-August-University
Andreas Janshoff: Institute for Physical Chemistry, Georg-August-University
Helmut Grubmüller: Max Planck Institute for Biophysical Chemistry
Herre J. Risselada: Max Planck Institute for Biophysical Chemistry
Christian Eggeling: Max Planck Institute for Biophysical Chemistry
Stefan W. Hell: Max Planck Institute for Biophysical Chemistry
Geert van den Bogaart: Max Planck Institute for Biophysical Chemistry
Reinhard Jahn: Max Planck Institute for Biophysical Chemistry

Nature Communications, 2015, vol. 6, issue 1, 1-10

Abstract: 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.

Date: 2015
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms6984

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DOI: 10.1038/ncomms6984

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