Group IVC cytosolic phospholipase A2gamma is farnesylated and palmitoylated in mammalian cells

doi:10.1194/jlr.M500230-JLR200

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A more recent version of this article appeared on October 1, 2005

Papers In Press, published online ahead of print August 1, 2005
J. Lipid Res., doi:10.1194/jlr.M500230-JLR200

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Submitted on June 7, 2005
Revised on July 22, 2005
Accepted on July 26, 2005

Group IVC cytosolic phospholipase A₂gamma is farnesylated and palmitoylated in mammalian cells

Dawn E. Tucker, Allison Stewart, Laxman Nallan, Pravine Bendale, Farideh Ghomashchi, Michael H. Gelb, and Christina C. Leslie

National Jewish Medical and Research Center, Denver, CO 80206

Corresponding Author: lesliec{at}njc.org

Cytosolic phospholipase A₂ gamma (cPLA₂ $gamma$ ) is a member of the Group IV family of intracellular PLA₂ enzymes, but unlike the well-studied cPLA₂ $alpha$ , is constitutively bound to membrane and is calcium independent. cPLA₂ $gamma$ contains a C-terminal CaaX sequence and is radiolabeled by mevalonic acid when expressed in cPLA₂ $alpha$ -deficient immortalized lung fibroblasts (IMLF^-/-). The radiolabel associated with cPLA₂ $gamma$ was identified as the farnesyl group. The protein farnesyltransferase inhibitor BMS-214662 prevented incorporation of [³H]mevalonic acid into cPLA₂ $gamma$ and partially suppressed serum-stimulated arachidonic acid release from IMLF^-/- and undifferentiated human skeletal muscle (SkMc) cells over-expressing cPLA₂ $gamma$ , but not from cells over-expressing cPLA₂ $alpha$ . However, BMS-214662 did not alter the amount of cPLA₂ $gamma$ associated with membrane. These results were consistent in COS cells expressing the C538S cPLA₂ $gamma$ prenylation mutant. cPLA₂ $gamma$ also contains a classic myristoylation site and several potential palmitoylation sites and was found to be acylated with oleic and palmitic acids but not myristoylated. Immunofluorescence microscopy revealed that cPLA₂ $gamma$ is associated with mitochondria in IMLF^-/-, SkMc cells and COS cells.

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