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 phospholipase D2a. Biochemical and Biophysical Research Communications, Vol.369 (No.2). pp. 478-484. ISSN 0006-291X

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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. (C) 2008 Elsevier Inc. All rights reserved.

Item Type:	Journal Article
Subjects:	Q Science > QD Chemistry Q Science > QH Natural history > QH301 Biology Q Science > QP Physiology
Divisions:	Faculty of Science > Life Sciences (2010- ) > Biological Sciences ( -2010)
Library of Congress Subject Headings (LCSH):	Phospholipases, Apoptosis
Journal or Publication Title:	Biochemical and Biophysical Research Communications
Publisher:	Elsevier
ISSN:	0006-291X
Date:	2 May 2008
Volume:	Vol.369
Number:	No.2
Number of Pages:	7
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:	Restricted or Subscription Access
Funder:	Biotechnology and Biological Sciences Research Council (Great Britain) (BBSRC)
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URI:	http://wrap.warwick.ac.uk/id/eprint/30310

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