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  Hydrophobic mismatch sorts SNARE proteins into distinct membrane domains.

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.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0025-6C39-A Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002A-19EE-D
Genre: Journal Article

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 Creators:
Milovanovic, D.1, Author              
Honigmann, A.1, Author              
Koike, S:, Author
Göttfert, F.1, Author              
Pahler, G., Author
Junius, M., Author
Müller, S., Author
Diederichsen, U., Author
Janshoff, A., Author
Grubmüller, H.2, Author              
Risselada, H. J.2, Author              
Eggeling, C.1, Author              
Hell, S. W.1, Author              
van den Bogaart, G.3, Author              
Jahn, R.3, Author              
Affiliations:
1Department of NanoBiophotonics, MPI for biophysical chemistry, Max Planck Society, ou_578627              
2Department of Theoretical and Computational Biophysics, MPI for biophysical chemistry, Max Planck Society, ou_578631              
3Department of Neurobiology, MPI for biophysical chemistry, Max Planck Society, ou_578595              

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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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Language(s): eng - English
 Dates: 2015-01-30
 Publication Status: Published online
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 Rev. Method: Peer
 Identifiers: DOI: 10.1038/ncomms6984
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Title: Nature Communications
Source Genre: Journal
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Pages: 10 Volume / Issue: 6 Sequence Number: 5984 Start / End Page: - Identifier: -