title: Membrane binding domains.
abstract: Eukaryotic signaling and trafficking proteins are rich in modular domains that bind cell membranes. These binding events are tightly regulated in space and time. The structural, biochemical, and biophysical mechanisms for targeting have been worked out for many families of membrane binding domains. This review takes a comparative view of seven major classes of membrane binding domains, the C1, C2, PH, FYVE, PX, ENTH, and BAR domains. These domains use a combination of specific headgroup interactions, hydrophobic membrane penetration, electrostatic surface interactions, and shape complementarity to bind to specific subcellular membranes.
authors.affiliation: Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, US Department of Health and Human Services, Bethesda, MD 20892, USA. hurley@helix.nih.gov
authors.forename: James H
authors.initials: JH
authors.lastname: Hurley
mesh_terms: D000818:Animals; D001665:Binding Sites / Q000502:physiology; D002462:Cell Membrane / Q000378:metabolism*; D006801:Humans; D057927:Hydrophobic and Hydrophilic Interactions; D050356:Lipid Metabolism; D008563:Membrane Lipids / Q000378:metabolism*; D008958:Models, Molecular; D017434:Protein Structure, Tertiary; D021381:Protein Transport; D015398:Signal Transduction
chemical_list: D008563:Membrane Lipids