The transmembrane domain of the SNARE protein VAMP2 is highly sensitive to its lipid environment
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 spectros...
| Автори: | , , , , , , , , |
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| Формат: | Journal article |
| Мова: | English |
| Опубліковано: |
Elsevier
2018
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| _version_ | 1826257511449100288 |
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| author | Fezoua-Boubegtiten, Z Hastoy, B Scotti, P Milochau, A Bathany, K Desbat, B Castano, S Oda, R Lang, J |
| author_facet | Fezoua-Boubegtiten, Z Hastoy, B Scotti, P Milochau, A Bathany, K Desbat, B Castano, S Oda, R Lang, J |
| author_sort | Fezoua-Boubegtiten, Z |
| collection | OXFORD |
| description | 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 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 G100/C103 within the transmembrane domain during lipid rearrangements in membrane fusion. |
| first_indexed | 2024-03-06T18:19:23Z |
| format | Journal article |
| id | oxford-uuid:05c416c0-7f88-4d9a-8392-52bff07d600f |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T18:19:23Z |
| publishDate | 2018 |
| publisher | Elsevier |
| record_format | dspace |
| spelling | oxford-uuid:05c416c0-7f88-4d9a-8392-52bff07d600f2022-03-26T08:58:49ZThe transmembrane domain of the SNARE protein VAMP2 is highly sensitive to its lipid environmentJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:05c416c0-7f88-4d9a-8392-52bff07d600fEnglishSymplectic Elements at OxfordElsevier2018Fezoua-Boubegtiten, ZHastoy, BScotti, PMilochau, ABathany, KDesbat, BCastano, SOda, RLang, JNeurotransmitter 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 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 G100/C103 within the transmembrane domain during lipid rearrangements in membrane fusion. |
| spellingShingle | Fezoua-Boubegtiten, Z Hastoy, B Scotti, P Milochau, A Bathany, K Desbat, B Castano, S Oda, R Lang, J The transmembrane domain of the SNARE protein VAMP2 is highly sensitive to its lipid environment |
| title | The transmembrane domain of the SNARE protein VAMP2 is highly sensitive to its lipid environment |
| title_full | The transmembrane domain of the SNARE protein VAMP2 is highly sensitive to its lipid environment |
| title_fullStr | The transmembrane domain of the SNARE protein VAMP2 is highly sensitive to its lipid environment |
| title_full_unstemmed | The transmembrane domain of the SNARE protein VAMP2 is highly sensitive to its lipid environment |
| title_short | The transmembrane domain of the SNARE protein VAMP2 is highly sensitive to its lipid environment |
| title_sort | transmembrane domain of the snare protein vamp2 is highly sensitive to its lipid environment |
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