ArticleMicrobiology (Reading, England)2015
In vivo characterization of the scaffold activity of flotillin on the membrane kinase KinC of Bacillus subtilis.
Article in Microbiology (Reading, England), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
What it found
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Who cites it
13 citing papers in PubMed, 33 citations in OpenAlex.
- Exploring the Diversity and Function of the SPFH-Domain Containing Proteins in Pseudomonas aeruginosa.Environmental microbiology reports · 2026Article
- The SPFH complex HflK-HflC regulates aerobic respiration in bacteria.PLoS biology · 2025Article
- Escherichia coli SPFH Membrane Microdomain Proteins HflKC Contribute to Aminoglycoside and Oxidative Stress Tolerance.Microbiology spectrum · 2023Article
- Article
- A carotenoid-deficient mutant of the plant-associated microbe Pantoea sp. YR343 displays an altered membrane proteome.Scientific reports · 2020Article
- Flotillin-mediated membrane fluidity controls peptidoglycan synthesis and MreB movement.eLife · 2020Article
- Impact of Fatty-Acid Labeling ofFrontiers in microbiology · 2020Article
- Article
- Flotillin scaffold activity contributes to type VII secretion system assembly in Staphylococcus aureus.PLoS pathogens · 2017Article
- Functional Membrane Microdomains Organize Signaling Networks in Bacteria.The Journal of membrane biology · 2017Review
- Attenuating Staphylococcus aureus Virulence by Targeting Flotillin Protein Scaffold Activity.Cell chemical biology · 2017Article
- Exploring functional membrane microdomains in bacteria: an overview.Current opinion in microbiology · 2017Review
- Shedding light on biology of bacterial cells.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2016Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 2 countries.
Funding
Abstract
Scaffold proteins are ubiquitous chaperones that bind to proteins and facilitate the physical interaction of the components of signal transduction pathways or multi-enzymic complexes. In this study, we used a biochemical approach to dissect the molecular mechanism of a membrane-associated scaffold protein, FloT, a flotillin-homologue protein that is localized in functional membrane microdomains of the bacterium Bacillus subtilis. This study provides unambiguous evidence that FloT physically binds to and interacts with the membrane-bound sensor kinase KinC. This sensor kinase activates biofilm formation in B. subtilis in response to the presence of the self-produced signal surfactin. Furthermore, we have characterized the mechanism by which the interaction of FloT with KinC benefits the activity of KinC. Two separate and synergistic effects constitute this mechanism: first, the scaffold activity of FloT promotes more efficient self-interaction of KinC and facilitates dimerization into its active form. Second, the selective binding of FloT to KinC prevents the occurrence of unspecific aggregation between KinC and other proteins that may generate dead-end intermediates that could titrate the activity of KinC. Flotillin proteins appear to play an important role in prokaryotes in promoting effective binding of signalling proteins with their correct protein partners.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.