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PLD2 is a peripheral membrane protein belonging to phospholipase D family with a PH domain, two PLD phosphodiesterase domains and a PX (phox homology) domain that plays a regulatory rather than catalytic role. PLD2 catalyzes the hydrolysis of phosphatidylcholine (PC) to produce phosphatidic acid and choline. PLD2 may function in regulated secretion, signal-induced cytoskeletal regulation and/or endocytosis, transcriptional regulation, and cell cycle control. It is usually stimulated by phosphatidylinositol 4,5-bisphosphate (PIP2) and activated by the ADP-ribosylation factor-1 (ARF-1). PLD2 is activated by agonist stimulation of both tyrosine kinase and G protein-coupled receptors and is also known to interact with EGFR and PIP5K1A. PLD2, localized to plasma membrane caveolae, is ubiquitously expressed in most tissues.
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