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Originally published In Press as doi:10.1074/jbc.M011368200 on February 14, 2001

J. Biol. Chem., Vol. 276, Issue 21, 18303-18312, May 25, 2001
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Phorbol Esters and Related Analogs Regulate the Subcellular Localization of beta 2-Chimaerin, a Non-protein Kinase C Phorbol Ester Receptor*

Maria J. CalocaDagger , HongBin WangDagger , Andrew DelemosDagger , Shaomeng Wang§, and Marcelo G. KazanietzDagger

From the Dagger  Center for Experimental Therapeutics and Department of Pharmacology, University of Pennsylvania School of Medicine, Philadelphia, Pennsylvania 19104-6160 and § Georgetown Institute for Cognitive and Computational Science, Georgetown University Medical Center, Washington, D.C. 20007

The novel phorbol ester receptor beta 2-chimaerin is a Rac-GAP protein possessing a single copy of the C1 domain, a 50-amino acid motif initially identified in protein kinase C (PKC) isozymes that is involved in phorbol ester and diacylglycerol binding. We have previously shown that, like PKCs, beta 2-chimaerin binds phorbol esters with high affinity in a phospholipid-dependent manner (Caloca, M. J., Fernandez, M. N., Lewin, N. E., Ching, D., Modali, R., Blumberg, P. M., and Kazanietz, M. G. (1997) J. Biol. Chem. 272, 26488-26496). In this paper we report that like PKC isozymes, beta 2-chimaerin is translocated by phorbol esters from the cytosolic to particulate fraction. Phorbol esters also induce translocation of alpha 1 (n)- and beta 1-chimaerins, suggesting common regulatory mechanisms for all chimaerin isoforms. The subcellular redistribution of beta 2-chimaerin by phorbol esters is entirely dependent on the C1 domain, as revealed by deletional analysis and site-directed mutagenesis. Interestingly, beta 2-chimaerin translocates to the Golgi apparatus after phorbol ester treatment, as revealed by co-staining with the Golgi marker BODIPY-TR-ceramide. Structure relationship analysis of translocation using a series of PKC ligands revealed substantial differences between translocation of beta 2-chimaerin and PKCalpha . Strikingly, the mezerein analog thymeleatoxin is not able to translocate beta 2-chimaerin, although it very efficiently translocates PKCalpha . Phorbol esters also promote the association of beta 2-chimaerin with Rac in cells. These data suggest that chimaerins can be positionally regulated by phorbol esters and that each phorbol ester receptor class has distinct pharmacological properties and targeting mechanisms. The identification of selective ligands for each phorbol ester receptor class represents an important step in dissecting their specific cellular functions.

* This work was supported by American Cancer Society Grant RPG-97-092-04-CNE and National Institutes of Health Grant RO1-CA74197-01.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed: Center for Experimental Therapeutics, University of Pennsylvania School of Medicine, 816 Biomedical Research Bldg. II/III, 421 Curie Blvd., Philadelphia, PA 19104-6160. E-mail: marcelo@spirit.gcrc.upenn.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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