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The transmembrane domain of the SNARE protein VAMP2 is highly sensitive to its lipid environment

dc.rights.licenseopenen_US
dc.contributor.authorFEZOUA-BOUBEGTITEN, Zahia
dc.contributor.authorHASTOY, Benoit
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorSCOTTI, Pier
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorMILOCHAU, Alexandra
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorBATHANY, Katell
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorDESBAT, Bernard
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorCASTANO, Sabine
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorODA, Reiko
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorLANG, Jochen
dc.date.accessioned2020-06-10T15:03:02Z
dc.date.available2020-06-10T15:03:02Z
dc.date.issued2019
dc.identifier.issn1879-2642en_US
dc.identifier.otherhttps://doi.org/10.1016/j.bbamem.2018.12.011en_US
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/7869
dc.description.abstractEnNeurotransmitter and hormone exocytosis depends on SNARE protein transmembrane domains and membrane lipids but their interplay is poorly understood. We investigated the interaction of the structure of VAMP2, a vesicular transmembrane SNARE protein, and membrane lipid composition by infrared spectroscopy using either the wild-type transmembrane domain (TMD), VAMP2TM22, or a peptide mutated at the central residues G100/C103 (VAMP2TM22VV) previously identified by us as being critical for exocytosis. Our data show that the structure of VAMP2TM22, in terms of alpha-helices and beta-sheets is strongly influenced by peptide/lipid ratios, by lipid species including cholesterol and by membrane surface charges. Differences observed in acyl chain alignments further underscore the role of the two central small amino acid residues G100/C103 within the transmembrane domain during lipid rearrangements in membrane fusion. Copyright © 2018 Elsevier B.V. All rights reserved.
dc.language.isoENen_US
dc.subject.enATR-infrared spectroscopy
dc.subject.enSynaptobrevin
dc.subject.enExocytosis
dc.subject.enSNARE proteins
dc.subject.enCholesterol
dc.subject.enPhospholipid
dc.title.enThe transmembrane domain of the SNARE protein VAMP2 is highly sensitive to its lipid environment
dc.typeArticle de revueen_US
dc.identifier.doi10.1016/j.bbamem.2018.12.011
dc.subject.halChimie/Matériauxen_US
bordeaux.journalBiochimica et Biophysica Acta:Biomembranesen_US
bordeaux.page670-676en_US
bordeaux.volume1861en_US
bordeaux.hal.laboratoriesInstitut de Chimie & de Biologie des Membranes & des Nano-objets (CBMN) - UMR 5248en_US
bordeaux.issue3en_US
bordeaux.institutionBordeaux INPen_US
bordeaux.institutionUniversité de Bordeauxen_US
bordeaux.peerReviewedouien_US
bordeaux.inpressnonen_US
hal.identifierhal-03182246
hal.version1
hal.date.transferred2021-03-29T08:39:31Z
hal.exporttrue
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