Subcellular targeting by membrane lipids.
The reversible localization of signaling proteins to both the plasma and the internal membranes of cells is critical for the selective activation of downstream functions and depends on interactions with both proteins and membrane lipids. New structural and biochemical analyses of C1, C2, PH, FYVE, FERM and other domains have led to an unprecedented amount of information on the molecular interactions of these signaling proteins with regulatory lipids. A wave of studies using GFP-tagged membrane binding domains as reporters has led to new quantitative insights into the kinetics of these signaling mechanisms.
Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892-0580, USA. jh8e@nih.gov
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JH
Hurley
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T
Meyer
D000818:Animals; D001692:Biological Transport; D002462:Cell Membrane / Q000378:metabolism*; D006801:Humans; D008563:Membrane Lipids / Q000378:metabolism*; D019269:Phosphatidylinositol 4,5-Diphosphate / Q000378:metabolism; D010716:Phosphatidylinositols / Q000378:metabolism; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry / Q000378:metabolism
D008563:Membrane Lipids; D019269:Phosphatidylinositol 4,5-Diphosphate; D010716:Phosphatidylinositols; D011506:Proteins