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Overview
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Background
Phosphatidylcholine phospholipase D1 and D2 (PC-PLD1 and PC-PLD2) are phospholipid-specific phosphodiesterases that hydrolyze phosphatidylcholine. Unlike PC-PLD1, which associates with secretory granules, PC-PLD2 localizes to the plasma membrane, where it is implicated in the formation of endocytotic vesicles. Both PC-PLD1 and PC-PLD2 coordinately regulate macrophage phagocytosis. PC-PLD activity in mammalian cells is transiently stimulated upon activation by G protein-coupled and receptor tyrosine kinase cell surface receptors. In addition, tubulin binding to PC-PLD2 inhibits muscarinic receptor-linked PC-PLD2 activation. PC-PLD2 also enhances PKCzeta activity through direct interaction in a lipase activity-independent manner.
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