JBC Transcription and Nuclear Factor Monoclonals

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Originally published In Press as doi:10.1074/jbc.M101983200 on April 27, 2001

J. Biol. Chem., Vol. 276, Issue 29, 27698-27708, July 20, 2001
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Effects of Protein Kinase CK2, Extracellular Signal-regulated Kinase 2, and Protein Phosphatase 2A on a Phosphatidic Acid-preferring Phospholipase A1*

May H. HanDagger , David K. M. Han§, Ruedi H. Aebersold, and John A. GlomsetDagger ||**Dagger Dagger

From the Dagger  Howard Hughes Medical Institute, || Departments of Medicine and Biochemistry, and ** Regional Primate Research Center, University of Washington, Seattle, Washington 98195-7370, the § Department of Physiology, University of Connecticut School of Medicine, Farmington, Connecticut 06030, and  Institute of Systems Biology, Seattle, Washington 98105-6099

A soluble, phosphatidic acid-preferring phospholipase A1, expressed in mature bovine testes but not in newborn calf testes, may contribute to the formation or function of sperm. Here we incubated a recombinant preparation of the phospholipase in vitro with several enzymes including protein kinase CK2 (CK2), extracellular signal-regulated kinase 2 (ERK2), and protein phosphatase 2A (PP2A) to identify effects that might be of regulatory importance in vivo. Major findings were that 1) CK2 phosphorylated the phospholipase on serines 93, 105, and 716; 2) ERK2 phosphorylated the enzyme on serine 730; 3) there was cross-antagonism between the reactions that phosphorylated serines 716 and 730; 4) PP2A selectively hydrolyzed phosphate groups that were esterified to serines 716 and 730; 5) CK2alpha formed a stable, MgATP/MgGTP-dependent complex with the phospholipase by a novel mechanism; and 6) the complex showed reduced phospholipase activity and resembled a complex identified in homogenates of macaque testis. These results provide the first available information about the effects of reactions of phosphorylation and dephosphorylation on the behavior of the phospholipase, shed light on properties of CK2alpha that may be required for the formation of complexes with its substrates, and raise the possibility that a complex containing CK2alpha and the phospholipase may play a special biological role in the testis.

* This work was supported by the Howard Hughes Medical Institute and by National Institutes of Health Grants RR00166, Al 34339, and RR 11823.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.

Dagger Dagger To whom all correspondence should be addressed: Howard Hughes Medical Institute Research Laboratories, University of Washington, Box 357370, Seattle, WA 98195-7370. Tel.: 206-685-2503; Fax: 206-616-1324; E-mail: jglomset@u.washington.edu.

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