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J Biol Chem, Vol. 273, Issue 32, 20261-20266, August 7, 1998

Mapping of a Molecular Determinant for Protein Kinase C _II Isozyme Function

Yesim Gökmen-Polar and Alan P. Fields^§¶

From the  Sealy Center for Oncology and Hematology and the Departments of ^§ Pharmacology and ^¶ Human Biological Chemistry and Genetics, University of Texas Medical Branch, Galveston, Texas 77555-1048

In human erythroleukemia (K562) cells, the highly related protein kinase C (PKC)  and PKC _II isozymes serve distinct functions in cellular differentiation and proliferation, respectively. Previous studies using two domain switch PKC chimera revealed that the catalytic domains of PKC  and _II contain molecular determinants important for isozyme-specific function (Walker, S. D., Murray, N. R., Burns, D. J., and Fields, A. P. (1995) Proc. Natl. Acad. Sci. U.S.A. 92, 9156-9160). We have now analyzed a panel of PKC chimeras to determine the specific region within the catalytic domain important for PKC _II function. A cellular assay for PKC _II function was devised based on the finding that PKC _II selectively translocates to the nucleus and phosphorylates nuclear lamin B in response to the PKC activator bryostatin. This response is strictly dependent upon expression of PKC _II or a PKC chimera that functions like PKC _II. We demonstrate that a PKC /_II chimera containing only the carboxyl-terminal 13 amino acids from PKC _II (_II V5) is capable of nuclear translocation and lamin B phosphorylation. These results are consistent with our recent observation that the PKC _II V5 region binds to phosphatidylglycerol (PG), a potent and selective PKC _II activator present in the nuclear membrane (Murray, N. R., and Fields, A. P. (1998) J. Biol. Chem. 273, 11514-11520). Soluble _II V5 peptide selectively inhibits PG-stimulated PKC _II activity in a dose-dependent fashion, indicating that PG-mediated activation of PKC _II involves interactions with the _II V5 region of the enzyme. We conclude that _II V5 is a major determinant for PKC _II nuclear function and suggest a model in which binding of PG to the _II V5 region stimulates nuclear PKC _II activity during G₂ phase of the cell cycle.

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Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.

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