cPLA2 is phosphorylated and activated by MAP kinase
Graduate School of Biomedical Sciences; Howard Hughes Medical Institute Department of Biochemistry and Molecular Biology; Program in Molecular Medicine
Life Sciences | Medicine and Health Sciences
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.
Cell. 1993 Jan 29;72(2):269-78.
Lin L, Wartmann M, Lin AY, Knop JL, Seth A, Davis RJ. (1993). cPLA2 is phosphorylated and activated by MAP kinase. Morningside Graduate School of Biomedical Sciences Student Publications. Retrieved from https://escholarship.umassmed.edu/gsbs_sp/763