Hydrophobic mismatch sorts SNARE proteins into distinct membrane domains

dc.bibliographicCitation.firstPage5984
dc.bibliographicCitation.journalTitleNature Communicationseng
dc.bibliographicCitation.volume6
dc.contributor.authorMilovanovic, Dragomir
dc.contributor.authorHonigmann, Alf
dc.contributor.authorKoike, Seiichi
dc.contributor.authorGöttfert, Fabian
dc.contributor.authorPähler, Gesa
dc.contributor.authorJunius, Meike
dc.contributor.authorMüllar, Stefan
dc.contributor.authorDiederichsen, Ulf
dc.contributor.authorJanshoff, Andreas
dc.contributor.authorGrubmüller, Helmut
dc.contributor.authorRisselada, Herre J.
dc.contributor.authorEggeling, Christian
dc.contributor.authorHell, Stefan W.
dc.contributor.authorvan den Bogaart, Geert
dc.contributor.authorJahn, Reinhard
dc.date.accessioned2022-07-29T07:11:02Z
dc.date.available2022-07-29T07:11:02Z
dc.date.issued2015
dc.description.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.eng
dc.description.versionpublishedVersioneng
dc.identifier.urihttps://oa.tib.eu/renate/handle/123456789/9822
dc.identifier.urihttp://dx.doi.org/10.34657/8860
dc.language.isoengeng
dc.publisher[London] : Nature Publishing Group UK
dc.relation.doihttps://doi.org/10.1038/ncomms6984
dc.relation.essn2041-1723
dc.rights.licenseCC BY 4.0 Unported
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/
dc.subject.ddc500
dc.subject.otherFluorescence Resonance Energy Transfereng
dc.subject.otherFluorescent Antibody Techniqueeng
dc.subject.otherHydrophobic and Hydrophilic Interactionseng
dc.subject.otherMolecular Dynamics Simulationeng
dc.subject.otherPhosphatidylinositolseng
dc.titleHydrophobic mismatch sorts SNARE proteins into distinct membrane domainseng
dc.typeArticleeng
dc.typeTexteng
tib.accessRightsopenAccesseng
wgl.contributorIOMger
wgl.subjectBiowissenschaften/Biologieger
wgl.subjectChemieger
wgl.typeZeitschriftenartikelger
Files
Original bundle
Now showing 1 - 1 of 1
Loading...
Thumbnail Image
Name:
Hydrophobic_mismatch_sorts_SNARE.pdf
Size:
1002.24 KB
Format:
Adobe Portable Document Format
Description: