Abstract
The recent identification of cDNA clones for phospholipase D1 and 2 has opened the door to new studies on its structure and regulation. PLD activity is encoded by at least two different genes that contain catalytic domains that relate their mechanism of action to phosphodiesterases. In vivo roles for PLD suggest that it may be important for multiple specialized steps in receptor dependent and constitutive processes of secretion, endocytosis, and membrane biogenesis.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
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Review
MeSH terms
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Amino Acid Sequence
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Animals
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Cell Line
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Conserved Sequence
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Enzyme Activation
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Enzyme Inhibitors / pharmacology
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Gene Expression Regulation, Enzymologic
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Mammals / genetics
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Mammals / metabolism*
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Phosphatidylinositol 4,5-Diphosphate / pharmacology
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Phosphatidylinositols / metabolism
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Phospholipase D / chemistry
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Phospholipase D / genetics
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Phospholipase D / metabolism*
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Protein Kinase C / pharmacology
Substances
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Enzyme Inhibitors
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Phosphatidylinositol 4,5-Diphosphate
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Phosphatidylinositols
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Protein Kinase C
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Phospholipase D