Molecular mechanisms behind remorin nanodomain formation by solidstate NMR
dc.rights.license | open | en_US |
hal.structure.identifier | Chimie et Biologie des Membranes et des Nanoobjets [CBMN] | |
dc.contributor.author | LEGRAND, Anthony | |
hal.structure.identifier | Chimie et Biologie des Membranes et des Nanoobjets [CBMN] | |
dc.contributor.author | MARTINEZ, Denis | |
dc.contributor.author | GRONNIER, Julien | |
hal.structure.identifier | Chimie et Biologie des Membranes et des Nanoobjets [CBMN] | |
dc.contributor.author | BERBON, Melanie | |
hal.structure.identifier | Chimie et Biologie des Membranes et des Nanoobjets [CBMN] | |
dc.contributor.author | DECOSSAS, Marion | |
dc.contributor.author | GOUGET, Paul | |
hal.structure.identifier | Laboratoire de biogenèse membranaire [LBM] | |
dc.contributor.author | GERMAIN, Veronique | |
hal.structure.identifier | Chimie et Biologie des Membranes et des Nanoobjets [CBMN] | |
dc.contributor.author | GRELARD, Axelle | |
hal.structure.identifier | Chimie et Biologie des Membranes et des Nanoobjets [CBMN] | |
dc.contributor.author | LAMBERT, Olivier | |
hal.structure.identifier | Chimie et Biologie des Membranes et des Nanoobjets [CBMN] | |
dc.contributor.author | LOQUET, Antoine | |
dc.contributor.author | MONGRAND, Sébastien | |
hal.structure.identifier | Chimie et Biologie des Membranes et des Nanoobjets [CBMN] | |
dc.contributor.author | HABENSTEIN, Birgit | |
dc.date.accessioned | 2021-06-30T15:06:16Z | |
dc.date.available | 2021-06-30T15:06:16Z | |
dc.date.issued | 2019 | |
dc.identifier.issn | 0175-7571 | en_US |
dc.identifier.uri | https://oskar-bordeaux.fr/handle/20.500.12278/94947 | |
dc.description.abstractEn | Protein and lipid components in biological membranes act as a dynamic network of subtle molecular inter-actions segregating the membrane into particular regions called nanodomains. Nanodomains act as func-tional platforms enriched in specific lipids (such as sterols and phosphoinositides) and proteins to performtheir diverse activities. Remorins (REMs) are plant proteins and well-established nanodomain markers and,as such, they can be considered as paradigm to provide a mechanistic description of membrane organisationinto functional nanodomains. Using solid-state nuclear magnetic resonance (ssNMR) and building upon ourinitial knowledge ofStREM1.3 and its C-terminal membrane anchor, we reveal the delicate balance betweenhydrophobic and electrostatic effects leading up to the protein’s characteristic affinity for negatively chargedphospholipids. In a divide-and-conquer approach, we describe the impact ofStREM1.3’s C-terminal anchor, itsoligomerisation domain and intrinsically disordered region on membrane structure and dynamics. Further-more, we tackle the structural features ofStREM1.3 when associated to nanodomain-mimicking membranes.We reveal thatStREM1.3 drives nanodomain organisation by concerted lipid-protein and protein-protein inter-actions | |
dc.language.iso | EN | en_US |
dc.subject.en | Solid-state NMR | |
dc.subject.en | Membrane | |
dc.subject.en | Nanodomains | |
dc.subject.en | Remorin | |
dc.title.en | Molecular mechanisms behind remorin nanodomain formation by solidstate NMR | |
dc.type | Article de revue | en_US |
dc.subject.hal | Chimie/Matériaux | en_US |
bordeaux.journal | European Biophysics Journal with Biophysics Letters | en_US |
bordeaux.page | S246-S246 | en_US |
bordeaux.volume | 48 | en_US |
bordeaux.hal.laboratories | Institut de Chimie & de Biologie des Membranes & des Nano-objets (CBMN) - UMR 5248 | en_US |
bordeaux.institution | Université de Bordeaux | en_US |
bordeaux.institution | Bordeaux INP | en_US |
bordeaux.institution | CNRS | |
bordeaux.peerReviewed | oui | en_US |
bordeaux.inpress | non | en_US |
hal.identifier | hal-03275111 | |
hal.version | 1 | |
hal.date.transferred | 2021-06-30T15:06:18Z | |
hal.export | true | |
bordeaux.COinS | ctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=European%20Biophysics%20Journal%20with%20Biophysics%20Letters&rft.date=2019&rft.volume=48&rft.spage=S246-S246&rft.epage=S246-S246&rft.eissn=0175-7571&rft.issn=0175-7571&rft.au=LEGRAND,%20Anthony&MARTINEZ,%20Denis&GRONNIER,%20Julien&BERBON,%20Melanie&DECOSSAS,%20Marion&rft.genre=article |
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