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Originally published In Press as doi:10.1074/jbc.M400770200 on April 5, 2004

J. Biol. Chem., Vol. 279, Issue 27, 28251-28256, July 2, 2004
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Isoenzyme-specific Translocation of Protein Kinase C (PKC){beta}II and not PKC{beta}I to a Juxtanuclear Subset of Recycling Endosomes

INVOLVEMENT OF PHOSPHOLIPASE D*

Kevin P. Becker and Yusuf A. Hannun{ddagger}

From the Department of Biochemistry and Molecular Biology, Medical University of South Carolina, Charleston, South Carolina 29425

Elucidation of isoenzyme-specific functions of individual protein kinase C (PKC) isoenzymes has emerged as an important goal in the study of this family of kinases, but this task has been complicated by modest substrate specificity and high homology among the individual members of each PKC subfamily. The classical PKC{beta}I and PKC{beta}II isoenzymes provide a unique opportunity because they are the alternatively spliced products of the {beta} gene and are 100% identical except for the last 50 of 52 amino acids. In this study, it is shown that green fluorescent protein-tagged PKC{beta}II and not PKC{beta}I translocates to a recently described juxtanuclear site of localization for PKC{alpha} and PKC{beta}II isoenzymes that arises with sustained stimulation of PKC. Mechanistically, translocation of PKC{beta}II to the juxtanuclear region required kinase activity. PKC{beta}II, but not PKC{beta}I, was found to activate phospholipase D within this time frame. Inhibitors of phospholipase D (1-butanol and a dominant negative construct) prevented the translocation of PKC{beta}II to the juxtanuclear region but not to the plasma membrane, thus demonstrating a role for phospholipase D in the juxtanuclear translocation of PKC{beta}II. Taken together, these results define specific biochemical and cellular actions of PKC{beta}II when compared with PKC{beta}I.

Received for publication, January 23, 2004 , and in revised form, March 29, 2004.

* This work was supported by National Institutes of Health Grant HL-43707 (to Y. A. H.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

{ddagger} To whom correspondence should be addressed: Dept. of Biochemistry and Molecular Biology, Medical University of South Carolina, 173 Ashley Ave., P. O. Box 250509, Charleston, SC 29425. Tel.: 843-792-4321; Fax: 843-792-4322; E-mail: hannun{at}musc.edu.


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