cPLA2 is phosphorylated and activated by MAP kinase.
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Lin LL, Wartmann M, Lin AY, Knopf JL, Seth A, Davis RJ
cPLA2 is phosphorylated and activated by MAP kinase.
Cell. 1993 Jan 29;72(2):269-78.
- PubMed ID
- 8381049 [ View in PubMed]
- Abstract
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.