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- W2023672273 abstract "Heterotrimeric GTP-binding (G) proteins transduce hormone-induced signals to their effector enzymes, which include several phospholipases. In particular, the G o /G i and G q protein families have been shown to couple signaling to phospholipase A 2 (PLA 2 ), phospholipase C, and phospholipase D, while the G 12 /G 13 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 G 12 /G 13 family is also able to activate cPLA 2 α, through the activation of RhoA and, subsequently, ERK1/2. Hormone-induced arachidonic acid release increased as a consequence of Gα 13 overexpression, and was inhibited through inhibition of Gα 13 signaling. The Gα 13 -mediated cPLA 2 α 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 cPLA 2 α regulation that is initiated by thrombin and purinergic receptor activation, and that signals through Gα 13 , RhoA and ERK1/2, with the involvement of a calyculin-sensitive phosphatase." @default.
- W2023672273 created "2016-06-24" @default.
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- W2023672273 date "2006-12-01" @default.
- W2023672273 modified "2023-09-25" @default.
- W2023672273 title "Gα13 mediates activation of the cytosolic phospholipase A2α through fine regulation of ERK phosphorylation" @default.
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- W2023672273 doi "https://doi.org/10.1016/j.cellsig.2006.05.003" @default.
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