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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. doi:10.1016/j.bbrc.2008.02.064 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 | ||||
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Subjects: | R Medicine > R Medicine (General) | ||||
Divisions: | Faculty of Science, Engineering and Medicine > Medicine > Warwick Medical School > Biomedical Sciences > Cell & Developmental Biology Faculty of Science, Engineering and Medicine > Medicine > Warwick Medical School |
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Library of Congress Subject Headings (LCSH): | Apoptosis, Phospholipase D | ||||
Journal or Publication Title: | Biochemical and Biophysical Research Communications | ||||
Publisher: | Elsevier | ||||
ISSN: | 0006-291x | ||||
Official Date: | 25 February 2008 | ||||
Dates: |
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Volume: | Vol.369 | ||||
Number: | No.2 | ||||
Page Range: | pp. 478-484 | ||||
DOI: | 10.1016/j.bbrc.2008.02.064 | ||||
Status: | Peer Reviewed | ||||
Publication Status: | Published | ||||
Access rights to Published version: | Open Access (Creative Commons) | ||||
Description: | Version accepted by publisher (post-print, after peer review, before copy-editing). |
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