Phospholipase D2 (PLD2)

Phospholipase D2 (PLD2) is a membrane-associated enzyme in humans encoded by the PLD2 gene. It catalyzes the hydrolysis of phosphatidylcholine to produce phosphatidic acid and choline, a reaction central to signal transduction and membrane dynamics. PLD2 is distinguished from the related isoform PLD1 by its constitutive enzymatic activity and predominant localization at the plasma membrane, where it modulates endocytosis, cytoskeletal organization, and cell signaling. PLD2 functions downstream of tyrosine kinase and G protein-coupled receptors, integrates into pathways regulating secretion, cell migration, and cytoskeletal rearrangement, and has demonstrated roles in pathological states including cancer, inflammation, bone diseases, and cardiovascular pathology[1][2][3][4]. Selective small-molecule PLD2 inhibitors are under investigation as tools for dissecting its biology and as potential therapeutics in disease contexts associated with aberrant PLD2 activity[1][2].

Other names

PLD2PLD 2hPLD2Choline phosphatase 2PLD1CPhosphatidylcholine-hydrolyzing phospholipase D2choline phosphatase 2

Inhibition of PLD2 enzymatic activity blocks the production of phosphatidic acid, reducing downstream signal transduction and processes such as cell migration, endocytosis, or cytoskeletal rearrangement[1][2][3]. Inhibition of PLD2 can interfere with receptor internalization and cellular signaling (e.g., Angiotensin II receptor endocytosis)[4].