Regulation of phospholipase D by tyrosine kinases.
Activation of phospholipase D (PLD) represents part of an important signalling pathway in mammalian cells. Phospholipase D catalyzed hydrolysis of phospholipids generates phosphatidic acid (PA) which is subsequently metabolized to lyso-PA (LPA) or diacylglycerol (DAG). While DAG is an endogenous activator of protein kinase C (PKC), PA and LPA have been recognized as second messengers as well. Activation of PLD in response to an external stimulus may involve PKC, Ca2+, G-proteins and/or tyrosine kinases. In this review, we will address the role of protein tyrosine phosphorylation in growth factor-, agonist- and oxidant-mediated activation of PLD. Furthermore, a possible link between PKC, Ca2+, G-proteins and tyrosine kinases is discussed to indicate the complexity involved in the regulation of PLD in mammalian cells.
Natarajan
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V
Department of Medicine, Indiana University School of Medicine, Indianapolis 46202, USA.
Scribner
W M
WM
Vepa
S
S
D000818:Animals; D004789:Enzyme Activation; D006801:Humans; D010739:Phospholipase D / Q000378:metabolism / Q000502:physiology*; D011505:Protein-Tyrosine Kinases / Q000378:metabolism / Q000502:physiology*; D015290:Second Messenger Systems / Q000502:physiology
D011505:Protein-Tyrosine Kinases; D010739:Phospholipase D