Publication | Closed Access
Phospholipase D: a Downstream Effector of ARF in Granulocytes
635
Citations
27
References
1994
Year
Proteinlipid InteractionCellular PhysiologyInflammationReceptor Tyrosine KinaseAutophagyCell SurfaceSecretory PathwayCell SignalingBiochemistryGranulocytePurified Arf ProteinsCell BiologyProtein PhosphorylationPhagocyteSignal TransductionPhospholipase DNatural SciencesIntracellular TraffickingCellular BiochemistrySystems BiologyMedicine
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.
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