FEZOUA-BOUBEGTITEN, Zahia; HASTOY, Benoit; SCOTTI, Pier; MILOCHAU, Alexandra; BATHANY, Katell; DESBAT, Bernard; CASTANO, Sabine; ODA, Reiko; LANG, Jochen

doi:10.1016/j.bbamem.2018.12.011

Metadatos

Mostrar el registro completo del ítem

Licencia de uso del documento

FEZOUA-BOUBEGTITEN, Zahia

HASTOY, Benoit

SCOTTI, Pier
Chimie et Biologie des Membranes et des Nanoobjets [CBMN]

Idioma

Article de revue

Este ítem está publicado en

Biochimica et Biophysica Acta:Biomembranes. 2019, vol. 1861, n° 3, p. 670-676

Resumen en inglés

Neurotransmitter 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.< Leer menos

Palabras clave en inglés

ATR-infrared spectroscopy

Synaptobrevin

Exocytosis

SNARE proteins

Cholesterol

Phospholipid

Metadatos

Compartir este ítem

Licencia de uso del documento

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

Idioma

Este ítem está publicado en

Resumen en inglés

Palabras clave en inglés

URI

DOI

Link to research data

Centros de investigación