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Papers In Press, published online ahead of print April 27, 2001
Howard Hughes Medical Institute, University of Washington, Seattle, WA 98195
Corresponding Author: jglomset{at}u.washington.edu
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) CK2
J. Biol. Chem, 10.1074/jbc.M101983200
Submitted on March 5, 2001
Revised on April 26, 2001
Accepted on April 27, 2001
Effects of protein kinase CK2, extracellular signal-regulated kinase 2, and protein phosphatase 2A on a phosphatidic acid-preferring phospholipase A1
formed a stable, MgATP/MgGTP-dependent complex with the phospholipase by a novel mechanism. 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 CK2 that may be required for the formation of complexes with its substrates, and raise the possibility that a complex containing CK2 and the phospholipase may play a special biological role in the testis.
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