Modeling the interplay between protein and lipid aggregation in supported membranes
[Display omitted] •We present a model that deals with lipid and protein segregation on surfaces.•Lipid segregation and active protein aggregation are not independent.•Lipid segregation affects filament shape, length and polymerization rate.•The lipid and protein time scale difference can give rise t...
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Veröffentlicht in: | Chemistry and physics of lipids 2015-01, Vol.185, p.141-152 |
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Hauptverfasser: | , , , , |
Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | [Display omitted]
•We present a model that deals with lipid and protein segregation on surfaces.•Lipid segregation and active protein aggregation are not independent.•Lipid segregation affects filament shape, length and polymerization rate.•The lipid and protein time scale difference can give rise to memory effects.•The model can be extended to include additional complexity in lipid behavior.
We present a theoretical model that deals with the complex interplay between lipid segregation and the self-aggregation of lipid-attached proteins. The model, in contrast to previous ones that consider proteins only as passive elements affecting the lipid distribution, describes the system including three terms: the dynamic interactions between protein monomers, the interactions between lipid components, and a mixed term considering protein–lipid interactions. It is used to explain experimental results performed on a well-defined system in which a self-aggregating soluble bacterial cytoskeletal protein polymerizes on a lipid bilayer containing two lipid components. All the elements considered in a previously described protein model, including torsion of the monomers within the filament, are needed to account for the observed filament shapes. The model also points out that lipid segregation can affect the length and curvature of the filaments and that the dynamic behavior of the lipids and proteins can have different time scales, giving rise to memory effects. This simple model that considers a dynamic protein assembly on a fluid and active lipid surface can be easily extended to other biologically relevant situations in which the interplay between protein and lipid aggregation is needed to fully describe the system. |
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ISSN: | 0009-3084 1873-2941 |
DOI: | 10.1016/j.chemphyslip.2014.06.006 |