cPLA2 is phosphorylated and activated by MAP kinase
| Autor: | John L. Knopf, Markus Wartmann, Alpna Seth, Alice Y. Lin, Lih-Ling Lin, Roger J. Davis |
|---|---|
| Rok vydání: | 1993 |
| Předmět: |
Phosphopeptides
CHO Cells Mitogen-activated protein kinase kinase Transfection Models Biological Peptide Mapping General Biochemistry Genetics and Molecular Biology Phospholipases A MAP2K7 Cell Line Phospholipase A2 Cytosol Cricetinae Serine Animals Receptors Platelet-Derived Growth Factor Amino Acid Sequence Phosphorylation Calcimycin Protein Kinase C MAPK14 MAP kinase kinase kinase biology Kinase Molecular biology Recombinant Proteins Enzyme Activation Kinetics Phospholipases A2 Mitogen-activated protein kinase Calcium-Calmodulin-Dependent Protein Kinases biology.protein Mutagenesis Site-Directed Tetradecanoylphorbol Acetate Calcium Protein Kinases |
| Zdroj: | Cell. 72(2) |
| ISSN: | 0092-8674 |
| Popis: | Treatment of cells with agents that stimulate the release of arachidonic acid causes increased serine phosphorylation and activation of cytosolic phospholipase A2 (cPLA2). Here we report that cPLA2 is a substrate for mitogen-activated protein (MAP) kinase. Moreover, phosphorylation by MAP kinase increases the enzymatic activity of cPLA2. The site of cPLA2 phosphorylation by MAP kinase, Ser-505, is identical to the major site of cPLA2 phosphorylation observed in phorbol ester-treated cells. Replacement of Ser-505 with Ala resulted in a mutant cPLA2 that is not a substrate for MAP kinase and causes little or no enhanced agonist-stimulated arachidonate release from intact cells. Taken together, these data indicate that MAP kinase mediates, at least in part, the agonist-induced activation of cPLA2. |
| Databáze: | OpenAIRE |
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