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Membranes (Basel). 2014 Jul 3;4(3):302-18. doi: 10.3390/membranes4030302.

Role of phospholipase d in g-protein coupled receptor function.

Author information

1
Department of Anatomy and Cell Biology, RWTH Aachen University, Wendlingweg 2, D-52074 Aachen, Germany. lbrandenburg@ukaachen.de.
2
Department of Anatomy and Cell Biology, RWTH Aachen University, Wendlingweg 2, D-52074 Aachen, Germany. tpufe@ukaachen.de.
3
Department of Pharmacology and Toxicology, Otto-von-Guericke-University Magdeburg, D-39120 Magdeburg, Germany. Thomkoc@gmx.de.

Abstract

Prolonged agonist exposure of many G-protein coupled receptors induces a rapid receptor phosphorylation and uncoupling from G-proteins. Resensitization of these desensitized receptors requires endocytosis and subsequent dephosphorylation. Numerous studies show the involvement of phospholipid-specific phosphodiesterase phospholipase D (PLD) in the receptor endocytosis and recycling of many G-protein coupled receptors e.g., opioid, formyl or dopamine receptors. The PLD hydrolyzes the headgroup of a phospholipid, generally phosphatidylcholine (PC), to phosphatidic acid (PA) and choline and is assumed to play an important function in cell regulation and receptor trafficking. Protein kinases and GTP binding proteins of the ADP-ribosylation and Rho families regulate the two mammalian PLD isoforms 1 and 2. Mammalian and yeast PLD are also potently stimulated by phosphatidylinositol 4,5-bisphosphate. The PA product is an intracellular lipid messenger. PLD and PA activities are implicated in a wide range of physiological processes and diseases including inflammation, diabetes, oncogenesis or neurodegeneration. This review discusses the characterization, structure, and regulation of PLD in the context of membrane located G-protein coupled receptor function.

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