Atypical PKCzeta is involved in RhoA-dependent mitogenic signaling by the P2Y(12) receptor in C6 cells

The FEBS Journal
Kristof Van Kolen, Herman Slegers

Abstract

When nucleotide hydrolysis is prevented, agonists of the P2Y(12) receptor enhance the proliferation of C6 glioma cells by RhoA-dependent, protein kinase C (PKC)-dependent activation of the extracellular signal-regulated kinase (ERK) pathway [Claes P, Grobben B, Van Kolen K, Roymans D & Slegers H (2001) Br J Pharmacol134, 402-408; Grobben B, Claes P, Van Kolen K, Roymans D, Fransen P, Sys SU & Slegers H (2001) J Neurochem78, 1325-1338]. In this study, we show that ERK1/2 phosphorylation was not affected by transfection of the cells with the Gbetagamma-subunit-scavenging adrenergic receptor kinase peptide [betaARK1-(495-689)] or with Rap1GAPII, indicating that P2Y(12) receptor stimulation enhances ERK1/2 phosphorylation by G(i)alpha subunit-mediated signaling independently of Rap1 activation. Inhibition of the RhoA downstream effector Rho-associated coiled-coil-containing kinase (ROCK) with Y-27632 did not affect the P2Y(12) receptor-induced increase in ERK1/2 phosphorylation but abrogated the mitogenic response. Involvement of growth factor receptor transactivation in the signaling towards ERK phosphorylation could be ruled out by the lack of an effect of PP2, AG1024, AG1296 or SU1498, inhibitors of Src, insulin-like growth fact...Continue Reading

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Citations

Feb 15, 2008·Naunyn-Schmiedeberg's Archives of Pharmacology·Laszlo KölesPeter Illes
Dec 28, 2006·Apoptosis : an International Journal on Programmed Cell Death·Eric LecainPatricia Crisanti
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Apr 6, 2019·Frontiers in Cell and Developmental Biology·Noelia Geribaldi-DoldánCarmen Castro

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