Abstract
Activation of the phospholipase D (PLD) pathway is a widespread response when cells are activated by agonists that bind receptors on the cell surface. A 16-kD cytosolic component can reconstitute guanosine triphosphate (GTP)-mediated activation of phospholipase D in HL60 cells depleted of their cytosol by permeabilization. This factor was purified and identified as two small GTP-binding proteins, ARF1 and ARF3. Recombinant ARF1 substituted for purified ARF proteins in the reconstitution assay. These results indicate that phospholipase D is a downstream effector of ARF1 and ARF3. The well-established role of ARF in vesicular traffic would suggest that alterations in lipid content by PLD are an important determinant in vesicular dynamics.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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ADP-Ribosylation Factor 1
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ADP-Ribosylation Factors
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Amino Acid Sequence
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Animals
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Cattle
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Cytosol / chemistry
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Enzyme Activation
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GTP-Binding Proteins / chemistry
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GTP-Binding Proteins / isolation & purification
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GTP-Binding Proteins / metabolism*
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Glycerophospholipids*
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Granulocytes / metabolism*
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Guanosine 5'-O-(3-Thiotriphosphate) / pharmacology
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Humans
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Molecular Sequence Data
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Phosphatidic Acids / metabolism
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Phosphatidylcholines / metabolism
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Phospholipase D / metabolism*
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Recombinant Proteins / metabolism
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Tumor Cells, Cultured
Substances
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Glycerophospholipids
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Phosphatidic Acids
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Phosphatidylcholines
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Recombinant Proteins
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phosphatidylethanol
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Guanosine 5'-O-(3-Thiotriphosphate)
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Phospholipase D
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GTP-Binding Proteins
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ADP-Ribosylation Factor 1
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ADP-Ribosylation Factors