When proteins that span the width of a cell's lipid membrane distort the membrane's shape, the proteins tend to aggregate in regions where membrane curvature helps to minimize such distortion. Such a curvature-driven mechanism of the localization of transmembrane proteins has been observed in vitro. However, experiments in vivo have supported an alternative model, where the clustering of the proteins is driven by stochastic nucleation. Now, H. Strahl et al. show that in the long-studied rod-shaped bacterium Bacillus subtilis, bacterial chemoreceptors (which in this case are protein complexes made of trimers of dimers that act as sensory clusters) accumulate at the highly curved membrane areas that are generated during cell division. The researchers find that it is indeed the curvature mismatch between the chemoreceptor trimers and the membrane (rather than stochastic clustering of the proteins) that is responsible for the aggregation of the protein complexes in highly curved membrane regions.
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Pámies, P. Sorted by curvature. Nature Mater 14, 1186 (2015). https://doi.org/10.1038/nmat4505
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DOI: https://doi.org/10.1038/nmat4505
