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A Central Small Amino Acid in the VAMP2 Transmembrane Domain Regulates the Fusion Pore in Exocytosis

hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorHASTOY, Benoit
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorSCOTTI, Pier-Arnaldo
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.authorFEZOUA-BOUBEGTITEN, Zahia
hal.structure.identifierLaboratoire de l'intégration, du matériau au système [IMS]
dc.contributor.authorRODAS, Jorge
hal.structure.identifierLaboratoire de l'intégration, du matériau au système [IMS]
dc.contributor.authorMEGRET, Remi
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.authorLAGUERRE, Michel
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorCASTANO, Sabine
dc.contributor.authorPERRAIS, D.
dc.contributor.authorRORSMAN, P.
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
IDREF: 085209600
dc.date.accessioned2020-07-09T14:16:51Z
dc.date.available2020-07-09T14:16:51Z
dc.date.issued2017-06
dc.identifier.issn2045-2322
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/10315
dc.description.abstractEnExocytosis depends on cytosolic domains of SNARE proteins but the function of the transmembrane domains (TMDs) in membrane fusion remains controversial. The TMD of the SNARE protein synaptobrevin2/VAMP2 contains two highly conserved small amino acids, G100 and C103, in its central portion. Substituting G100 and/or C103 with the beta-branched amino acid valine impairs the structural flexibility of the TMD in terms of alpha-helix/beta-sheet transitions in model membranes (measured by infrared reflection-absorption or evanescent wave spectroscopy) during increase in protein/lipid ratios, a parameter expected to be altered by recruitment of SNAREs at fusion sites. This structural change is accompanied by reduced membrane fluidity (measured by infrared ellipsometry). The G100V/C103V mutation nearly abolishes depolarization-evoked exocytosis (measured by membrane capacitance) and hormone secretion (measured biochemically). Single-vesicle optical (by TIRF microscopy) and biophysical measurements of ATP release indicate that G100V/C103V retards initial fusion-pore opening, hinders its expansion and leads to premature closure in most instances. We conclude that the TMD of VAMP2 plays a critical role in membrane fusion and that the structural mobility provided by the central small amino acids is crucial for exocytosis by influencing the molecular re-arrangements of the lipid membrane that are necessary for fusion pore opening and expansion.
dc.title.enA Central Small Amino Acid in the VAMP2 Transmembrane Domain Regulates the Fusion Pore in Exocytosis
dc.title.alternativeScientific reports
dc.typeArticle de revue
dc.identifier.doi10.1038/s41598-017-03013-3
dc.subject.halChimie/Matériaux
bordeaux.journalSci Rep
bordeaux.page2835
bordeaux.volume7
bordeaux.hal.laboratoriesInstitut de Chimie & de Biologie des Membranes & des Nano-objets (CBMN) - UMR 5248*
bordeaux.hal.laboratoriesInstitut de Chimie & de Biologie des Membranes & des Nano-objets (CBMN, UMR 5248)
bordeaux.issue1
bordeaux.institutionUniversité de Bordeaux
bordeaux.institutionBordeaux INP
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