AI Article Synopsis
- Neurotransmitter and hormone release relies on SNARE proteins and lipids, but their interaction is not well understood.
- The study focused on VAMP2, a key SNARE protein, examining how its structure is affected by different membrane lipid compositions using infrared spectroscopy.
- Findings revealed that the structure of VAMP2 is significantly influenced by the ratio of peptides to lipids, lipid types (like cholesterol), and membrane surface charges, highlighting the importance of specific amino acids in facilitating membrane fusion.
Article Abstract
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), VAMP2, or a peptide mutated at the central residues G/C (VAMP2VV) previously identified by us as being critical for exocytosis. Our data show that the structure of VAMP2, in terms of α-helices and β-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 G/C within the transmembrane domain during lipid rearrangements in membrane fusion.
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| http://dx.doi.org/10.1016/j.bbamem.2018.12.011 | DOI Listing |
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