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- W2086562476 abstract "The 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." @default.
- W2086562476 created "2016-06-24" @default.
- W2086562476 creator A5017784230 @default.
- W2086562476 date "2008-07-15" @default.
- W2086562476 modified "2023-09-30" @default.
- W2086562476 title "Molecular Mechanisms of PLD Function in Membrane Traffic" @default.
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- W2086562476 doi "https://doi.org/10.1111/j.1600-0854.2008.00742.x" @default.
- W2086562476 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/18422860" @default.
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