title: Protein-protein interactions and the spatiotemporal dynamics of bacterial outer membrane proteins.
abstract: 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.
authors.affiliation: Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK. Electronic address: colin.kleanthous@bioch.ox.ac.uk.
authors.forename: Colin
authors.initials: C
authors.lastname: Kleanthous
authors.affiliation: Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
authors.forename: Patrice
authors.initials: P
authors.lastname: Rassam
authors.affiliation: Department of Biology, University of York, York YO10 5DD, UK. Electronic address: christoph.baumann@york.ac.uk.
authors.forename: Christoph G
authors.initials: CG
authors.lastname: Baumann
mesh_terms: D001425:Bacterial Outer Membrane Proteins / Q000378:metabolism*; D002462:Cell Membrane / Q000378:metabolism; D006090:Gram-Negative Bacteria / Q000166:cytology / Q000378:metabolism; D025941:Protein Interaction Mapping / Q000379:methods*; D062211:Spatio-Temporal Analysis; D013379:Substrate Specificity
chemical_list: D001425:Bacterial Outer Membrane Proteins