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MBC in Press, published online ahead of print November 30, 2005
Mol. Biol. Cell 10.1091/mbc.E04-12-1100

A more recent version of this article appeared on February 1, 2006
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Submitted on December 21, 2004
Revised on October 27, 2005
Accepted on November 21, 2005

Targeting of PKC-{epsilon} during Fc{gamma}R-dependent Phagocytosis Requires the {epsilon}C1B Domain and Phospholipase C-{gamma}1

Keylon L. Cheeseman,* Takehiko Ueyama,{dagger} Tanya M. Michaud,* Kaori Kashiwagi,{dagger} Demin Wang,{ddagger} Lindsay A. Flax,* Yasuhito Shirai,{dagger} Daniel J. Loegering,{sect} Naoaki Saito,{dagger} and Michelle R. Lennartz*

Centers for *Cell Biology and Cancer Research and {sect}Cardiovascular Sciences, Albany Medical College, Albany, NY 12208; {dagger}Laboratory of Molecular Pharmacology, Biosignal Research Center, Kobe University, Nada- Ku, Kobe 657- 8501, Japan; {ddagger}The Blood Research Institute, The Blood Center of Southeastern Wisconsin, Milwaukee, WI 53226

Monitoring Editor: Vivek Malhotra

Protein Kinase C-{epsilon} (PKC-{epsilon}) translocates to phagosomes and promotes uptake of IgG-opsonized targets. To identify the regions responsible for this concentration, GFP-protein kinase C-{epsilon} mutants were tracked during phagocytosis and in response to exogenous lipids. Deletion of the diacylglycerol (DAG)-binding {epsilon}C1 and {epsilon}C1B domains, or the {epsilon}C1B point mutant {epsilon}C259G, decreased accumulation at phagosomes and membrane translocation in response to exogenous DAG. Quantitation of GFP revealed that {epsilon}C259G, {epsilon}C1, and {epsilon}C1B accumulation at phagosomes was significantly less than that of intact PKC-{epsilon}. Also, the DAG antagonist EI-150 blocked PKC-{epsilon} translocation. Thus DAG, binding to {epsilon}C1B, is necessary for PKC-{epsilon} translocation. The role of PLD, PI-PLC-{gamma}1 and PI-PLC-{gamma}2 in PKC-{epsilon} accumulation was assessed. Although GFP-PLD2 localized to phagosomes and enhanced phagocytosis, PLD inhibition did not alter target ingestion or PKC-{epsilon} localization. In contrast, the PI-PLC inhibitor U73122 decreased both phagocytosis and PKC-{epsilon} accumulation. Although expression of PI-PLC-{gamma}2 is higher than that of PI-PLC-{gamma}1, PI-PLC-{gamma}1, but not PI-PLC-{gamma}2, consistently concentrated at phagosomes. Macrophages from PI-PLC-{gamma}2-/- mice were similar to wild type macrophages in their rate and extent of phagocytosis, their accumulation of PKC-{epsilon} at the phagosome, and their sensitivity to U73122. This implicates PI-PLC-{gamma}1 as the enzyme that supports PKC-{epsilon} localization and phagocytosis. The fact that PI-PLC-{gamma}1 was transiently tyrosine phosphorylated in nascent phagosomes is consistent with this conclusion. Taken together, these results support a model in which PI-PLC-{gamma}1 provides DAG that binds to {epsilon}C1B, facilitating PKC-{epsilon} localization to phagosomes for efficient IgG-mediated phagocytosis.

Address correspondence to: Michelle R. Lennartz (lennarm{at}mail.amc.edu)




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