title: Lipid metabolism and regulation of membrane trafficking.
abstract: The past 20 years have witnessed tremendous progress in our understanding of the molecular machinery that controls protein and membrane transport between organelles (Scheckman R, Orci L. Coat proteins and vesicle budding. Science 1996;271: 1526-1533 and Rothman JE. Mechanisms of intracellular protein transport. Nature 1994;372: 55-63.) The research efforts responsible for these impressive advances have largely focused on the identification and characterization of protein factors that participate in membrane trafficking events. The role of membranes and their lipid constituents has received considerably less attention. Indeed, until rather recently, popular models for mechanisms of membrane trafficking had relegated membrane lipids to the status of a passive platform, subject to deformation by the action of coat proteins whose polymerization and depolymerization govern vesicle budding and fusion reactions. The 1990s, and particularly its last half, has brought fundamental reappraisals of the interface of lipids and lipid metabolism in regulating intracellular membrane trafficking events. Some of the emerging themes are reviewed here.
authors.affiliation: Department of Cell Biology, University of Alabama at Birmingham, Birmingham, AL 35294-0005, USA.
authors.forename: R P
authors.initials: RP
authors.lastname: Huijbregts
authors.forename: L
authors.initials: L
authors.lastname: Topalof
authors.forename: V A
authors.initials: VA
authors.lastname: Bankaitis
mesh_terms: D019870:1-Phosphatidylinositol 4-Kinase / Q000378:metabolism; D000818:Animals; D001692:Biological Transport / Q000502:physiology*; D002352:Carrier Proteins / Q000502:physiology; D022163:Clathrin-Coated Vesicles / Q000378:metabolism; D004705:Endocytosis; D005089:Exocytosis; D005656:Fungal Proteins / Q000378:metabolism; D006801:Humans; D008051:Lipid Bilayers; D008322:Mammals / Q000378:metabolism; D008563:Membrane Lipids / Q000378:metabolism*; D008565:Membrane Proteins / Q000378:metabolism; D051379:Mice; D018345:Mice, Knockout; D008954:Models, Biological; D010713:Phosphatidylcholines / Q000378:metabolism; D043265:Phosphatidylinositol Diacylglycerol-Lyase; D010716:Phosphatidylinositols / Q000378:metabolism; D049294:Phospholipid Transfer Proteins; D010744:Phosphoric Monoester Hydrolases / Q000378:metabolism; D021381:Protein Transport / Q000502:physiology; D012441:Saccharomyces cerevisiae / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins; D010738:Type C Phospholipases / Q000378:metabolism
chemical_list: D002352:Carrier Proteins; D005656:Fungal Proteins; D008051:Lipid Bilayers; D008563:Membrane Lipids; D008565:Membrane Proteins; D010713:Phosphatidylcholines; D010716:Phosphatidylinositols; D049294:Phospholipid Transfer Proteins; C118289:SEC24 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins; D019870:1-Phosphatidylinositol 4-Kinase; C441760:PIK1 protein, S cerevisiae; D010744:Phosphoric Monoester Hydrolases; C053087:inositol-1,4-bisphosphate 1-phosphatase; D010738:Type C Phospholipases; D043265:Phosphatidylinositol Diacylglycerol-Lyase