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cPLA2 is phosphorylated and activated by MAP kinase

L L Lin1, M Wartmann, A Y Lin

  • 1Genetics Institute, Small Molecule Drug Discovery Group, Cambridge, Massachusetts 02140.

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|January 29, 1993
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Mitogen-activated protein (MAP) kinase phosphorylates and activates cytosolic phospholipase A2 (cPLA2) at Ser-505. This MAP kinase-mediated activation is crucial for agonist-induced arachidonic acid release in cells.

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Area of Science:

  • Cellular signaling pathways
  • Enzymology
  • Molecular biology

Background:

  • Agonist stimulation triggers arachidonic acid release, involving cytosolic phospholipase A2 (cPLA2) activation and serine phosphorylation.
  • The precise mechanisms regulating cPLA2 activation remain incompletely understood.

Purpose of the Study:

  • To investigate the role of mitogen-activated protein (MAP) kinase in the activation of cPLA2.
  • To identify the specific phosphorylation site on cPLA2 targeted by MAP kinase.

Main Methods:

  • In vitro kinase assays to determine if cPLA2 is a substrate for MAP kinase.
  • Site-directed mutagenesis to replace the identified phosphorylation site (Ser-505) with alanine.
  • Assessment of cPLA2 enzymatic activity and arachidonic acid release in cells expressing wild-type and mutant cPLA2.

Main Results:

  • cPLA2 was identified as a direct substrate for MAP kinase.
  • Phosphorylation of cPLA2 by MAP kinase significantly increased its enzymatic activity.
  • Serine-505 was identified as the primary site of MAP kinase-mediated phosphorylation on cPLA2.
  • A mutant cPLA2 with Ser-505 replaced by alanine was not phosphorylated by MAP kinase and showed significantly reduced agonist-stimulated arachidonic acid release.

Conclusions:

  • MAP kinase plays a significant role in mediating the agonist-induced activation of cPLA2.
  • Phosphorylation of cPLA2 at Ser-505 by MAP kinase is a key step in regulating arachidonic acid release.