13 mediates activation of the cytosolic phospholipase A2α through fine regulation of ERK phosphorylation

Stefania Mariggiò, Aljosa Bavec, Elena Natale, Pasquale Zizza, Mario Salmona, Daniela Corda, Maria Di Girolamo

Research output: Contribution to journalArticlepeer-review


Heterotrimeric GTP-binding (G) proteins transduce hormone-induced signals to their effector enzymes, which include several phospholipases. In particular, the Go/Gi and Gq protein families have been shown to couple signaling to phospholipase A2 (PLA2), phospholipase C, and phospholipase D, while the G12/G13 family has been linked to the activation of small GTPases of the Rho family, and hence, to phospholipase D activation. Here, we demonstrate that in CHO cells, the G12/G13 family is also able to activate cPLA2α, through the activation of RhoA and, subsequently, ERK1/2. Hormone-induced arachidonic acid release increased as a consequence of Gα13 overexpression, and was inhibited through inhibition of Gα13 signaling. The Gα13-mediated cPLA2α activation was inhibited by pharmacological blockade of ERK1/2 with either U0126 or PD98059, and by RhoA inactivation with C3 toxin or a dominant-negative RhoA (N19RhoA), and was stimulated by the serine-threonine phosphatase inhibitor calyculin A. Our data thus identify a pathway of cPLA2α regulation that is initiated by thrombin and purinergic receptor activation, and that signals through Gα13, RhoA and ERK1/2, with the involvement of a calyculin-sensitive phosphatase.

Original languageEnglish
Pages (from-to)2200-2208
Number of pages9
JournalCellular Signalling
Issue number12
Publication statusPublished - Dec 2006


  • Arachidonic acid
  • ATP
  • CHO cells
  • cPLA
  • G proteins
  • G-protein-coupled receptors
  • Mitogen-activated protein kinase
  • Thrombin

ASJC Scopus subject areas

  • Cell Biology


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