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Identification of caspase 3 motifs and critical aspartate residues in human Phospholipase D1b and Phopsholipase D2a

By Michelle H. Wright, Michelle J. Farquhar, Mina-Olga Aletrari, Graham Ladds and Matthew N. Hodgkin

Abstract

Stimulation of mammalian cells frequently initiates phospholipase D-catalysed\ud hydrolysis of phosphatidylcholine in the plasma membrane to yield phosphatidic acid\ud (PA) a novel lipid messenger. PA plays a regulatory role in important cellular\ud processes such as secretion, cellular shape change and movement. A number of\ud studies have highlighted that PLD-based signalling also plays a pro-mitogenic and\ud pro-survival role in cells and therefore anti-apoptotic. We show that human PLD1b\ud and PLD2a contain functional caspase-3 cleavage sites and identify the critical\ud aspartate residues within PLD1b that affect its activation by phorbol esters and\ud attenuate phosphatidylcholine hydrolysis during apoptosis

Topics: R1
Publisher: Elsevier
Year: 2008
OAI identifier: oai:wrap.warwick.ac.uk:106

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