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The Role of Membrane-Mediated Interactions in the Assembly and Architecture of Chemoreceptor Lattices

Author(s): Haselwandter, Christoph; Wingreen, Ned

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Abstract: In vivo fluorescence microscopy and electron cryo-tomography have revealed that chemoreceptors self-assemble into extended honeycomb lattices of chemoreceptor trimers with a well-defined relative orientation of trimers. The signaling response of the observed chemoreceptor lattices is remarkable for its extreme sensitivity, which relies crucially on cooperative interactions among chemoreceptor trimers. In common with other membrane proteins, chemoreceptor trimers are expected to deform the surrounding lipid bilayer, inducing membrane-mediated anisotropic interactions between neighboring trimers. Here we introduce a biophysical model of bilayer-chemoreceptor interactions, which allows us to quantify the role of membrane-mediated interactions in the assembly and architecture of chemoreceptor lattices. We find that, even in the absence of direct protein-protein interactions, membrane-mediated interactions can yield assembly of chemoreceptor lattices at very dilute trimer concentrations. The model correctly predicts the observed honeycomb architecture of chemoreceptor lattices as well as the observed relative orientation of chemoreceptor trimers, suggests a series of ‘‘gateway’’ states for chemoreceptor lattice assembly, and provides a simple mechanism for the localization of large chemoreceptor lattices to the cell poles. Our model of bilayer-chemoreceptor interactions also helps to explain the observed dependence of chemotactic signaling on lipid bilayer properties. Finally, we consider the possibility that membrane-mediated interactions might contribute to cooperativity among neighboring chemoreceptor trimers
Publication Date: 11-Dec-2014
Electronic Publication Date: 11-Dec-2014
Citation: Haselwandter, Christoph A, Wingreen, Ned S. (2014). The Role of Membrane-Mediated Interactions in the Assembly and Architecture of Chemoreceptor Lattices. PLoS Computational Biology, 10 (12), e1003932 - e1003932. doi:10.1371/journal.pcbi.1003932
DOI: doi:10.1371/journal.pcbi.1003932
EISSN: 1553-7358
Pages: e1003932 - e1003932
Type of Material: Journal Article
Journal/Proceeding Title: PLoS Computational Biology
Version: Final published version. This is an open access article.

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