Identification of caspase 3 motifs and critical aspartate residues in human phospholipase D1b and phospholipase D2a.
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.
Wright
Michelle H
MH
Department of Biological Sciences, University of Warwick, Coventry West Midlands CV4 7AL, UK.
Farquhar
Michelle J
MJ
Aletrari
Mina-Olga
MO
Ladds
Graham
G
Hodgkin
Matthew N
MN
D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D017209:Apoptosis / Q000502:physiology; D001224:Aspartic Acid / Q000737:chemistry / Q000378:metabolism*; D053148:Caspase 3 / Q000737:chemistry* / Q000378:metabolism*; D002460:Cell Line; D006801:Humans; D007668:Kidney / Q000166:cytology* / Q000378:metabolism*; D008969:Molecular Sequence Data; D010739:Phospholipase D / Q000737:chemistry* / Q000378:metabolism*; D011485:Protein Binding
D001224:Aspartic Acid; D010739:Phospholipase D; C106801:phospholipase D1; D053148:Caspase 3