Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1935916 | Biochemical and Biophysical Research Communications | 2008 | 7 Pages |
Abstract
Stimulation of mammalian cells frequently initiates phospholipase D-catalyzed hydrolysis of phosphatidylcholine in the plasma membrane to yield phosphatidic acid (PA) a novel lipid messenger. PA plays a regulatory role in important cellular processes such as secretion, cellular shape change, and movement. A number of studies have highlighted that PLD-based signaling also plays a pro-mitogenic and pro-survival role in cells and therefore anti-apoptotic. We show that human PLD1b and PLD2a contain functional caspase 3 cleavage sites and identify the critical aspartate residues within PLD1b that affect its activation by phorbol esters and attenuate phosphatidylcholine hydrolysis during apoptosis.
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Authors
Michelle H. Wright, Michelle J. Farquhar, Mina-olga Aletrari, Graham Ladds, Matthew N. Hodgkin,