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J Biol Chem, Vol. 274, Issue 31, 21995-22001, July 30, 1999

Activation of Phospholipase C delta 1 through C2 Domain by a Ca2+-Enzyme-Phosphatidylserine Ternary Complex

Jon W. LomasneyDagger , Hwei-Fang Cheng§, Steve R. Roffler§, and Klim King§

From the Dagger  Feinberg Cardiovascular Research Institute, Departments of Pathology and Pharmacology, Northwestern University Medical School, Chicago, Illinois 60611 and the § Institute of Biomedical Sciences, Academia Sinica, Taipei 11529, Taiwan, Republic of China

The concentration of free Ca2+ and the composition of nonsubstrate phospholipids profoundly affect the activity of phospholipase C delta 1 (PLCdelta 1). The rate of PLCdelta 1 hydrolysis of phosphatidylinositol 4,5-bisphosphate was stimulated 20-fold by phosphatidylserine (PS), 4-fold by phosphatidic acid (PA), and not at all by phosphatidylethanolamine or phosphatidylcholine (PC). PS reduced the Ca2+ concentration required for half-maximal activation of PLCdelta 1 from 5.4 to 0.5 µM. In the presence of Ca2+, PLCdelta 1 specifically bound to PS/PC but not to PA/PC vesicles in a dose-dependent and saturable manner. Ca2+ also bound to PLCdelta 1 and required the presence of PS/PC vesicles but not PA/PC vesicles. The free Ca2+ concentration required for half-maximal Ca2+ binding was estimated to be 8 µM. Surface dilution kinetic analysis revealed that the Km was reduced 20-fold by the presence of 25 mol % PS, whereas Vmax and Kd were unaffected. Deletion of amino acid residues 646-654 from the C2 domain of PLCdelta 1 impaired Ca2+ binding and reduced its stimulation and binding by PS. Taken together, the results suggest that the formation of an enzyme-Ca2+-PS ternary complex through the C2 domain increases the affinity for substrate and consequently leads to enzyme activation.

Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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