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

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Wright, Michelle H., Farquhar, Michelle J., Aletrari, Mina-Olga , Ladds, Graham and Hodgkin, Matthew N.. (2008) Identification of caspase 3 motifs and critical aspartate residues in human Phospholipase D1b and Phopsholipase D2a. Biochemical and Biophysical Research Communications, Vol.369 (No.2). pp. 478-484. ISSN 0006-291x

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Official URL: http://dx.doi.org/10.1016/j.bbrc.2008.02.064

Abstract

Stimulation of mammalian cells frequently initiates phospholipase D-catalysed 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 signalling 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.

Item Type: Journal Article
Subjects: R Medicine > R Medicine (General)
Divisions: Faculty of Medicine > Warwick Medical School > Biomedical Cell Biology
Faculty of Medicine > Warwick Medical School
Library of Congress Subject Headings (LCSH): Apoptosis, Phospholipase D
Journal or Publication Title: Biochemical and Biophysical Research Communications
Publisher: Elsevier
ISSN: 0006-291x
Date: 25 February 2008
Volume: Vol.369
Number: No.2
Page Range: pp. 478-484
Identification Number: 10.1016/j.bbrc.2008.02.064
Status: Peer Reviewed
Publication Status: Published
Access rights to Published version: Open Access
Description: Version accepted by publisher (post-print, after peer review, before copy-editing).
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URI: http://wrap.warwick.ac.uk/id/eprint/106

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