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Papers In Press, published online ahead of print December 6, 2002
UPR 9023, Centre National de la Recherche Scientifique (CNRS), Montpellier, Cedex 05 34094
Corresponding Author: journot{at}montp.inserm.fr
The small GTPases Ras or Rap1 were suggested to mediate the stimulatory effect of some G protein-coupled receptors (GPCRs) on ERK activity in neuronal cells. Accordingly, we reported here that Pituitary Adenylate Cyclase-Activating Polypeptide (PACAP), whose GPCR triggers neuronal differentiation of the PC12 cell line via ERK1/2 activation, transiently activated Ras and induced the sustained GTP-loading of Rap1. Ras mediated peak stimulation of ERK by PACAP, whereas Rap1 was necessary for the sustained activation phase. However, PACAP-induced GTP-loading of Rap1 was not sufficient to account for ERK activation by PACAP since [1] PACAP-elicited Rap1 GTP-loading depended only on PLC whereas maximal stimulation of ERK by PACAP also required the activity of PKA, PKC and calcium-dependent signaling, and [2] constitutively active mutants of Rap1, Rap1A-V12 and Rap1B-V12, only minimally stimulated the ERK pathway compared to Ras-V12. The effect of Rap1A-V12 was dramatically potentiated by the concurrent activation of PKC, the cAMP pathway and Ras, and this potentiation was blocked by dominant-negative mutants of Ras and Raf. Thus, this set of data indicated that GPCR-elicited GTP-loading of Rap1 was not sufficient to efficiently stimulate ERK in PC12 cells, and required the permissive co-stimulation of PKA, PKC or Ras.
J. Biol. Chem, 10.1074/jbc.M204652200
Submitted on May 13, 2002
Revised on December 4, 2002
Accepted on December 6, 2002
Stimulation of the ERK pathway by GTP-loaded Rap1 requires the concomitant activation of Ras, PKC and PKA in neuronal cells ^
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