Nanodomain Clustering of the Plant Protein Remorin by Solid-State NMR
Nanodomains are dynamic membrane subcompartments, enriched in specific lipid, and protein components that act as functional platforms to manage an abundance of cellular processes. The remorin protein of plants is a well-established nanodomain marker and widely serves as a paradigm to study nanodomai...
| Main Authors: | , , , , , , , , |
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| Format: | Article |
| Language: | English |
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Frontiers Media S.A.
2019-10-01
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| Series: | Frontiers in Molecular Biosciences |
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| Online Access: | https://www.frontiersin.org/article/10.3389/fmolb.2019.00107/full |
| _version_ | 1818544450997059584 |
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| author | Anthony Legrand Anthony Legrand Denis Martinez Axelle Grélard Melanie Berbon Estelle Morvan Arpita Tawani Antoine Loquet Sébastien Mongrand Birgit Habenstein |
| author_facet | Anthony Legrand Anthony Legrand Denis Martinez Axelle Grélard Melanie Berbon Estelle Morvan Arpita Tawani Antoine Loquet Sébastien Mongrand Birgit Habenstein |
| author_sort | Anthony Legrand |
| collection | DOAJ |
| description | Nanodomains are dynamic membrane subcompartments, enriched in specific lipid, and protein components that act as functional platforms to manage an abundance of cellular processes. The remorin protein of plants is a well-established nanodomain marker and widely serves as a paradigm to study nanodomain clustering. Located at the inner leaflet of the plasma membrane, remorins perform essential functions during signaling. Using deuterium and phosphorus solid-state NMR, we inquire on the molecular determinants of the lipid-protein and protein-protein interactions driving nanodomain clustering. By monitoring thermotropism properties, lipid acyl chain order and membrane thickness, we report the effects of phosphoinositides and sterols on the interaction of various remorin peptides and protein constructs with the membrane. We probed several critical residues involved in this interaction and the involvement of the coiled-coil homo-oligomerisation domain into the formation of remorin nanodomains. We trace the essential role of the pH in nanodomain clustering based on anionic lipids such as phosphoinositides. Our results reveal a complex interplay between specific remorin residues and domains, the environmental pH and their resulting effects on the lipid dynamics for phosphoinositide-enriched membranes. |
| first_indexed | 2024-12-11T22:48:39Z |
| format | Article |
| id | doaj.art-c18fcf3dc0c44b88afbe23e8f376fca1 |
| institution | Directory Open Access Journal |
| issn | 2296-889X |
| language | English |
| last_indexed | 2024-12-11T22:48:39Z |
| publishDate | 2019-10-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Molecular Biosciences |
| spelling | doaj.art-c18fcf3dc0c44b88afbe23e8f376fca12022-12-22T00:47:32ZengFrontiers Media S.A.Frontiers in Molecular Biosciences2296-889X2019-10-01610.3389/fmolb.2019.00107482247Nanodomain Clustering of the Plant Protein Remorin by Solid-State NMRAnthony Legrand0Anthony Legrand1Denis Martinez2Axelle Grélard3Melanie Berbon4Estelle Morvan5Arpita Tawani6Antoine Loquet7Sébastien Mongrand8Birgit Habenstein9Institute of Chemistry & Biology of Membranes & Nanoobjects (UMR5248 CBMN), IECB, CNRS, Université Bordeaux, Institut Polytechnique Bordeaux, Pessac, FranceLaboratoire de Biogenèse Membranaire - UMR 5200 - CNRS, Université de Bordeaux, Villenave-d'Ornon, FranceInstitute of Chemistry & Biology of Membranes & Nanoobjects (UMR5248 CBMN), IECB, CNRS, Université Bordeaux, Institut Polytechnique Bordeaux, Pessac, FranceInstitute of Chemistry & Biology of Membranes & Nanoobjects (UMR5248 CBMN), IECB, CNRS, Université Bordeaux, Institut Polytechnique Bordeaux, Pessac, FranceInstitute of Chemistry & Biology of Membranes & Nanoobjects (UMR5248 CBMN), IECB, CNRS, Université Bordeaux, Institut Polytechnique Bordeaux, Pessac, FranceEuropean Institute of Chemistry and Biology - UMS3033/US001, Pessac, FranceInstitute of Chemistry & Biology of Membranes & Nanoobjects (UMR5248 CBMN), IECB, CNRS, Université Bordeaux, Institut Polytechnique Bordeaux, Pessac, FranceInstitute of Chemistry & Biology of Membranes & Nanoobjects (UMR5248 CBMN), IECB, CNRS, Université Bordeaux, Institut Polytechnique Bordeaux, Pessac, FranceLaboratoire de Biogenèse Membranaire - UMR 5200 - CNRS, Université de Bordeaux, Villenave-d'Ornon, FranceInstitute of Chemistry & Biology of Membranes & Nanoobjects (UMR5248 CBMN), IECB, CNRS, Université Bordeaux, Institut Polytechnique Bordeaux, Pessac, FranceNanodomains are dynamic membrane subcompartments, enriched in specific lipid, and protein components that act as functional platforms to manage an abundance of cellular processes. The remorin protein of plants is a well-established nanodomain marker and widely serves as a paradigm to study nanodomain clustering. Located at the inner leaflet of the plasma membrane, remorins perform essential functions during signaling. Using deuterium and phosphorus solid-state NMR, we inquire on the molecular determinants of the lipid-protein and protein-protein interactions driving nanodomain clustering. By monitoring thermotropism properties, lipid acyl chain order and membrane thickness, we report the effects of phosphoinositides and sterols on the interaction of various remorin peptides and protein constructs with the membrane. We probed several critical residues involved in this interaction and the involvement of the coiled-coil homo-oligomerisation domain into the formation of remorin nanodomains. We trace the essential role of the pH in nanodomain clustering based on anionic lipids such as phosphoinositides. Our results reveal a complex interplay between specific remorin residues and domains, the environmental pH and their resulting effects on the lipid dynamics for phosphoinositide-enriched membranes.https://www.frontiersin.org/article/10.3389/fmolb.2019.00107/fullnanodomainslipid raftsolid-state NMRmembrane proteinplant proteinphosphoinositide |
| spellingShingle | Anthony Legrand Anthony Legrand Denis Martinez Axelle Grélard Melanie Berbon Estelle Morvan Arpita Tawani Antoine Loquet Sébastien Mongrand Birgit Habenstein Nanodomain Clustering of the Plant Protein Remorin by Solid-State NMR Frontiers in Molecular Biosciences nanodomains lipid raft solid-state NMR membrane protein plant protein phosphoinositide |
| title | Nanodomain Clustering of the Plant Protein Remorin by Solid-State NMR |
| title_full | Nanodomain Clustering of the Plant Protein Remorin by Solid-State NMR |
| title_fullStr | Nanodomain Clustering of the Plant Protein Remorin by Solid-State NMR |
| title_full_unstemmed | Nanodomain Clustering of the Plant Protein Remorin by Solid-State NMR |
| title_short | Nanodomain Clustering of the Plant Protein Remorin by Solid-State NMR |
| title_sort | nanodomain clustering of the plant protein remorin by solid state nmr |
| topic | nanodomains lipid raft solid-state NMR membrane protein plant protein phosphoinositide |
| url | https://www.frontiersin.org/article/10.3389/fmolb.2019.00107/full |
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