ArticlePLoS genetics2016
Super Resolution Fluorescence Microscopy and Tracking of Bacterial Flotillin (Reggie) Paralogs Provide Evidence for Defined-Sized Protein Microdomains within the Bacterial Membrane but Absence of Clusters Containing Detergent-Resistant Proteins.
Article in PLoS genetics, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 54 citations in OpenAlex.
- Exploring the Diversity and Function of the SPFH-Domain Containing Proteins in Pseudomonas aeruginosa.Environmental microbiology reports · 2026Article
- Flotillin-mediated stabilization of unfolded proteins in bacterial membrane microdomains.Nature communications · 2024Article
- Protein secretion zones during overexpression of amylase within the Gram-positive cell wall.BMC biology · 2023Article
- Escherichia coli SPFH Membrane Microdomain Proteins HflKC Contribute to Aminoglycoside and Oxidative Stress Tolerance.Microbiology spectrum · 2023Article
- Bacterial lipid biophysics and membrane organization.Current opinion in microbiology · 2023Review
- Cross-linking of the endolysosomal system reveals potential flotillin structures and cargo.Nature communications · 2022Article
- Mycobacterial resistance to zinc poisoning requires assembly of P-ATPase-containing membrane metal efflux platforms.Nature communications · 2022Article
- How Does the Spatial Confinement of FtsZ to a Membrane Surface Affect Its Polymerization Properties and Function?Frontiers in microbiology · 2022Review
- The SPFH Protein Superfamily in Fungi: Impact on Mitochondrial Function and Implications in Virulence.Microorganisms · 2021Review
- Dynamics of Bacterial Signal Recognition Particle at a Single Molecule Level.Frontiers in microbiology · 2021Article
- Mini Review: Bacterial Membrane Composition and Its Modulation in Response to Stress.Frontiers in molecular biosciences · 2021Review
- Application of PALM Superresolution Microscopy to the Analysis of Microtubule-Organizing Centers (MTOCs) in Aspergillus nidulans.Methods in molecular biology (Clifton, N.J.) · 2021Article
- An Stomatin, Prohibitin, Flotillin, and HflK/C-Domain Protein Required to Link the Phage-Shock Protein to the Membrane inFrontiers in microbiology · 2021Article
- Article
- Flotillin-mediated membrane fluidity controls peptidoglycan synthesis and MreB movement.eLife · 2020Article
- TnApplied and environmental microbiology · 2020Article
- Impact of Fatty-Acid Labeling ofFrontiers in microbiology · 2020Article
- Complex Diffusion in Bacteria.Advances in experimental medicine and biology · 2020Review
- Visualization of Bacterial Protein Complexes Labeled with Fluorescent Proteins and Nanobody Binders for STED Microscopy.International journal of molecular sciences · 2019Article
- Microdomain formation is a general property of bacterial membrane proteins and induces heterogeneity of diffusion patterns.BMC biology · 2018Article
Corrections and comments
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Authors and funding
15 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Biological membranes have been proposed to contain microdomains of a specific lipid composition, in which distinct groups of proteins are clustered. Flotillin-like proteins are conserved between pro-and eukaryotes, play an important function in several eukaryotic and bacterial cells, and define in vertebrates a type of so-called detergent-resistant microdomains. Using STED microscopy, we show that two bacterial flotillins, FloA and FloT, form defined assemblies with an average diameter of 85 to 110 nm in the model bacterium Bacillus subtilis. Interestingly, flotillin microdomains are of similar size in eukaryotic cells. The soluble domains of FloA form higher order oligomers of up to several hundred kDa in vitro, showing that like eukaryotic flotillins, bacterial assemblies are based in part on their ability to self-oligomerize. However, B. subtilis paralogs show significantly different diffusion rates, and consequently do not colocalize into a common microdomain. Dual colour time lapse experiments of flotillins together with other detergent-resistant proteins in bacteria show that proteins colocalize for no longer than a few hundred milliseconds, and do not move together. Our data reveal that the bacterial membrane contains defined-sized protein domains rather than functional microdomains dependent on flotillins. Based on their distinct dynamics, FloA and FloT confer spatially distinguishable activities, but do not serve as molecular scaffolds.
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