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It has until recently been unclear whether outer membrane proteins (OMPs) of Gram-negative bacteria are organized or distributed randomly. Studies now suggest promiscuous protein-protein interactions (PPIs) between β-barrel OMPs in Escherichia coli govern their local and global dynamics, engender spatiotemporal patterning of the outer membrane into micro-domains and are the basis of β-barrel protein turnover. We contextualize these latest advances, speculate on areas of bacterial cell biology that might be influenced by the organization of OMPs into supramolecular assemblies, and highlight the new questions and controversies this revised view of the bacterial outer membrane raises.

Original publication




Journal article


Curr Opin Struct Biol

Publication Date





109 - 115


Bacterial Outer Membrane Proteins, Cell Membrane, Gram-Negative Bacteria, Protein Interaction Mapping, Spatio-Temporal Analysis, Substrate Specificity