AI Article Synopsis
- The study identifies the first human cDNA for phosphatidylcholine-specific phospholipase D (PLD), highlighting its role in key cellular processes like signal transduction and membrane trafficking.
- Recombinant human PLD1 is shown to be membrane-associated, preferentially acting on phosphatidylcholine, and influenced by other molecules such as phosphatidylinositol 4,5-bisphosphate and ADP-ribosylation factor-1.
- PLD1 is believed to represent the main gene responsible for the most researched endogenous PLD activity, indicating its importance in cellular functions.
Article Abstract
Activation of phosphatidylcholine-specific phospholipase D (PLD) has been implicated as a critical step in numerous cellular pathways, including signal transduction, membrane trafficking, and the regulation of mitosis. We report here the identification of the first human PLD cDNA, which defines a new and highly conserved gene family. Characterization of recombinant human PLD1 reveals that it is membrane-associated, selective for phosphatidylcholine, stimulated by phosphatidylinositol 4,5-bisphosphate, activated by the monomeric G-protein ADP-ribosylation factor-1, and inhibited by oleate. PLD1 likely encodes the gene product responsible for the most widely studied endogenous PLD activity.
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| http://dx.doi.org/10.1074/jbc.270.50.29640 | DOI Listing |
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