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J. Biol. Chem., Vol. 277, Issue 26, 23116-23122, June 28, 2002

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Selective Association of Protein Kinase C with 14-3-3  in Neuronally Differentiated PC12 Cells
STIMULATORY AND INHIBITORY EFFECT OF 14-3-3  IN VIVO^*

Laura Gannon-Murakami and Kentaro Murakami

From the Department of Biology, University of Vermont, Burlington, Vermont 05405

The 14-3-3 protein is a family of highly conserved acidic proteins found in a wide range of eukaryotes from yeast to mammals. 14-3-3 acts as an adapter protein and interacts with signaling molecules including protein kinase C (PKC). Although 14-3-3  was originally characterized as an endogenous PKC inhibitor, it was reported to activate PKC in vitro, but the in vivo regulation of PKC by 14-3-3 is still not well understood. To examine the regulation of PKC by 14-3-3 in the cell, we have generated a sub-cell line, PC12-B3, that stably expresses FLAG epitope-tagged 14-3-3  isoform in PC12 cells. Here we show that PKC- and PKC- become associated with 14-3-3  when the cells are neuronally differentiated by nerve growth factor. We found that the immunoprecipitate by anti-FLAG antibody contains constitutive and autonomous Ca²⁺-independent non-classical PKC activity. In contrast, the FLAG immunoprecipitate has no Ca²⁺-dependent classical PKC activity despite the fact that PKC- is present in the FLAG immunoprecipitate from differentiated PC12-B3 cells. Our results show that the association with 14-3-3  has distinct effects on classical PKC and non-classical PKC activity.

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