Bacterial flotillins as destabilizers of phospholipid membranes

From archaea to mammals evolutionary conserved flotillins are scaffolding proteins, recognized for their nandomain-segregating activity. Flotillins form basket-like oligomeric architectures on the membrane, based on a conserved secondary structure composition of the monomeric subunits: a membrane-targeting region, an SPFH domain and a coiled-coil "flotillin" domain. In B. subtilis, the two flotillins FloT and FloA are present, localizing mainly in distinct nanodomains and executing multiple cellular functions. We here use deuterium and phosphorus solid-state NMR to monitor the effect of the different flotillins FloT and FloA and their structural components on model membranes. We find a clear disordering effect of FloT and FloA on the membranes reaching the carbon positions in the centre of the membrane. This effect is imposed by the hydrophobic region and the adjacent SPFH domain and, surprisingly, further supported by the membrane-distant flotillin domain. Biological implications of this disordering action are discussed.

Authors

Institutions

Publication Details

Journal
Biochimica et Biophysica Acta (BBA) - Biomembranes
Published
2024-11-08
DOI
https://doi.org/10.1016/j.bbamem.2024.184399
Citations
6
Primary Topic
Caveolin-1 and cellular processes
Type
article
Field-Weighted Citation Impact
1.96

Funders

Controls
|||
ALL TIME
JAN
FEB
MAR
APR
MAY
JUN
JUL
AUG
SEP
OCT
article

Bacterial flotillins as destabilizers of phospholipid membranes

Estelle Morvan, Marc Bramkamp, Abigail Savietto Scholz, Dênis Martinez et al.
6 citations
Biochimica et Biophysica Acta (BBA) - Biomembranes
Caveolin-1 and cellular processes
1.96
article

Bacterial flotillins as destabilizers of phospholipid membranes

Estelle Morvan, Marc Bramkamp, Abigail Savietto Scholz, Dênis Martinez, Érick J. Dufourc, Mélanie Berbon, Ana Álvarez‐Mena, Axelle Grélard, Birgit Habenstein, Sarah Turpin
article en
6 citations

Abstract

From archaea to mammals evolutionary conserved flotillins are scaffolding proteins, recognized for their nandomain-segregating activity. Flotillins form basket-like oligomeric architectures on the membrane, based on a conserved secondary structure composition of the monomeric subunits: a membrane-targeting region, an SPFH domain and a coiled-coil "flotillin" domain. In B. subtilis, the two flotillins FloT and FloA are present, localizing mainly in distinct nanodomains and executing multiple cellular functions. We here use deuterium and phosphorus solid-state NMR to monitor the effect of the different flotillins FloT and FloA and their structural components on model membranes. We find a clear disordering effect of FloT and FloA on the membranes reaching the carbon positions in the centre of the membrane. This effect is imposed by the hydrophobic region and the adjacent SPFH domain and, surprisingly, further supported by the membrane-distant flotillin domain. Biological implications of this disordering action are discussed.

Biochimica et Biophysica Acta (BBA) - BiomembranesVol. 1867(1)
Centre National de la Recherche Scientifique (FR), Université de Bordeaux (FR), Inserm (FR), Hochschule für Angewandte Wissenschaften Kiel (DE), Christian-Albrechts-Universität zu Kiel (DE), Chimie et Biologie des Membranes et des Nanoobjects (FR), Institut Européen de Chimie et Biologie (FR), Institut Polytechnique de Bordeaux (FR)
Deutsche Forschungsgemeinschaft, Agence Nationale de la Recherche, Institut National de la Santé et de la Recherche Médicale, Centre National de la Recherche Scientifique
Openalex Percentile: Top 15%
Caveolin-1 and cellular processes
1.96
AI Navigator

Ask Laika to Summarize, Analyze, and Connect papers live on the map.

Summarize Papers & Methodologies

Extract key findings, datasets, and comparative methods across publications.

Benchmark Rankings & Visual Analytics

Rank top research institutions, authors, funders, topics, and journals by Field-Weighted Citation Impact (FWCI) and paper volume with instant charts.

Connect Distant Disciplines

Bridge topological clusters on the map to find hidden collaborative intersections.