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Using supported bilayers to study the spatiotemporal organization of membrane-bound proteins. | LitMetric

AI Article Synopsis

  • Cell division in prokaryotes and eukaryotes involves specific proteins binding to the cell membrane, which can be hard to study in living cells.
  • The article outlines methods for using supported lipid bilayers to replicate cell division mechanisms in E. coli and Xenopus laevis eggs, enabling detailed analysis of membrane proteins.
  • These techniques can also be applied to investigate other complex cellular processes like signaling, vesicle trafficking, and cell movement.

Article Abstract

Cell division in prokaryotes and eukaryotes is commonly initiated by the well-controlled binding of proteins to the cytoplasmic side of the cell membrane. However, a precise characterization of the spatiotemporal dynamics of membrane-bound proteins is often difficult to achieve in vivo. Here, we present protocols for the use of supported lipid bilayers to rebuild the cytokinetic machineries of cells with greatly different dimensions: the bacterium Escherichia coli and eggs of the vertebrate Xenopus laevis. Combined with total internal reflection fluorescence microscopy, these experimental setups allow for precise quantitative analyses of membrane-bound proteins. The protocols described to obtain glass-supported membranes from bacterial and vertebrate lipids can be used as starting points for other reconstitution experiments. We believe that similar biochemical assays will be instrumental to study the biochemistry and biophysics underlying a variety of complex cellular tasks, such as signaling, vesicle trafficking, and cell motility.

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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4578691PMC
http://dx.doi.org/10.1016/bs.mcb.2015.01.007DOI Listing

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