AI Article Synopsis
- Flotillins are scaffolding proteins that play a key role in organizing membranes in various organisms, from archaea to mammals, with a complex structure consisting of multiple functional domains.
- In the bacterium B. subtilis, the flotillins FloT and FloA localize to specific nanodomains and have various cellular functions, impacting membrane organization.
- Research using NMR techniques reveals that FloT and FloA can cause disorder in model membranes, affecting their structure and function, with implications for understanding cellular processes.
Article 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.
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| http://dx.doi.org/10.1016/j.bbamem.2024.184399 | DOI Listing |
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