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MBC in Press, published online ahead of print September 5, 2003
Mol. Biol. Cell 10.1091/mbc.E03-05-0295

A more recent version of this article appeared on December 1, 2003
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Submitted on May 13, 2003
Revised on July 3, 2003
Accepted on August 6, 2003

The simultaneous production of PtdOH and DAG is essential for the translocation of PKC{epsilon} to the plasma membrane in RBL-2H3 cells

Maria Jose Lopez-Andreo1, Juan C. Gomez-Fernandez1, and Senena Corbalan-Garcia1*

1 Dept. de Bioquímica y Biología Molecular (A). Facultad de Veterinaria, Universidad de Murcia, Apdo. 4021, E-30100 Murcia, Spain

* Corresponding author. E-mail address: senena{at}um.es.

To evaluate the role of the C2 domain in PKC{epsilon} localization and activation after stimulation of the IgE receptor in RBL-2H3 cells, we used a series of mutants located in the phospholipid binding region of the enzyme. The results obtained suggest that the interaction of the C2 domain with the phospholipids in the plasma membrane is essential for anchoring the enzyme in this cellular compartment. Furthermore, the use of specific inhibitors of the different pathways that generate both diacylglycerol and phosphatidic acid has shown that the phosphatidic acid generated via PLD-dependent pathway, in addition to the diacylglycerol generated via PI-PLCs, are involved in the localization of PKC{epsilon} in the plasma membrane. Direct stimulation of RBL-2H3 cells with very low concentrations of permeable phosphatidic acid and diacylglycerol exerted a synergistic effect on the plasma membrane localization of PKC{epsilon}. Moreover, the in vitro kinase assays showed that both phosphatidic acid and diacylglycerol are essential for enzyme activation. Taken together, these results demonstrate that phosphatidic acid is an important and essential activator of PKC{epsilon} through the C2 domain and locate this isoenzyme in a new scenario where it acts as a downstream target of PLD.




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