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.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.