cPLA2 is phosphorylated and activated by MAP kinase.

Article Details

Citation

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.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Cytosolic phospholipase A2P47712Details