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Vol. 10, Issue 11, 3863-3876, November 1999
Department of Pharmacological Sciences and Institute for Cell and
Developmental Biology, State University of New York, Stony Brook, New
York 11794-8651
Phosphatidylcholine (PC) is a major source of lipid-derived second
messenger molecules that function as both intracellular and
extracellular signals. PC-specific phospholipase D (PLD) and phosphatidic acid phosphohydrolase (PAP) are two pivotal enzymes in
this signaling system, and they act in series to generate the biologically active lipids phosphatidic acid (PA) and diglyceride. The
identity of the PAP enzyme involved in PLD-mediated signal transduction
is unclear. We provide the first evidence for a functional role of a
type 2 PAP, PAP2b, in the metabolism of PLD-generated PA. Our data
indicate that PAP2b localizes to regions of the cell in which PC
hydrolysis by PLD is taking place. Using a newly developed PAP2b-specific antibody, we have characterized the expression, posttranslational modification, and localization of endogenous PAP2b.
Glycosylation and localization of PAP2b appear to be cell type and
tissue specific. Biochemical fractionation and immunoprecipitation analyses revealed that PAP2b and PLD2 activities are present in caveolin-1-enriched detergent-resistant membrane microdomains. We
found that PLD2 and PAP2b act sequentially to generate diglyceride within this specialized membrane compartment. The unique lipid composition of these membranes may provide a selective environment for
the regulation and actions of enzymes involved in signaling through PC hydrolysis.
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