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- W2898864068 abstract "Abstract Many membrane remodeling events rely on the ability of curvature-generating N-BAR membrane proteins to organize into distinctive supramolecular configurations. Experiments have revealed a conformational switch in N-BAR proteins resulting in vesicular or tubular membrane shapes, with shallow membrane immersion of the H0 amphipathic helices of N-BAR proteins on vesicles but deep H0 immersion on tubes. We develop here a minimal elastic model of the local thinning of the lipid bilayer resulting from H0 immersion. Our model predicts that the observed conformational switch in N-BAR proteins produces a corresponding switch in the bilayer-mediated N-BAR interactions due to the H0 helices. In agreement with experiments, we find that bilayer-mediated H0 interactions oppose N-BAR multimerization for the shallow H0 membrane immersion depths measured on vesicles, but promote self-assembly of supramolecular N-BAR chains for the increased H0 membrane immersion depths measured on tubes. Finally, we consider the possibility that bilayer-mediated H0 interactions might contribute to the concerted structural reorganization of N-BAR proteins suggested by experiments. Our results indicate that the membrane immersion depth of amphipathic protein helices may provide a general molecular control parameter for membrane organization." @default.
- W2898864068 created "2018-11-09" @default.
- W2898864068 creator A5003327124 @default.
- W2898864068 creator A5013429613 @default.
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- W2898864068 date "2018-11-06" @default.
- W2898864068 modified "2023-10-12" @default.
- W2898864068 title "Directed Supramolecular Organization of N-BAR Proteins through Regulation of H0 Membrane Immersion Depth" @default.
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- W2898864068 doi "https://doi.org/10.1038/s41598-018-34273-2" @default.
- W2898864068 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6219572" @default.
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