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Molecular mechanisms of PLD function in membrane traffic Roth MGTraffic 2008[Aug]; 9 (8): 1233-9The two mammalian phosphatidylcholine (PC)-selective phospholipase D (PLD) enzymes remove the choline head group from PC to produce phosphatidic acid (PA). PA stimulates phosphatidylinositol(4)phosphate 5-kinases, can function as a binding site for membrane proteins, is required for certain membrane fusion or fission events and is an important precursor for the production of diacylglycerol (DAG). Both PA and DAG are lipids that favor negatively curved membranes rather than planar bilayers and can reduce the energetic barrier to membrane fission and fusion. Recent data provide a mechanistic explanation for the role PLDs play in some aspects of membrane traffic and provide an explanation for why some membrane fusion reactions require PA and some do not. PLDs also act as guanosine triphosphatase-activating proteins for dynamin and may participate with dynamin in the process of vesicle fission.|Animals[MESH]|Catalytic Domain[MESH]|Cell Membrane/*enzymology/metabolism[MESH]|Dynamins/metabolism[MESH]|Guanosine Triphosphate/chemistry/metabolism[MESH]|Humans[MESH]|Lipid Bilayers/chemistry[MESH]|Lipids/chemistry[MESH]|Models, Biological[MESH]|Phospholipase D/*metabolism[MESH]|Phosphotransferases (Alcohol Group Acceptor)/metabolism[MESH]|Protein Transport[MESH]|Saccharomyces cerevisiae/metabolism[MESH] |
