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Molecular and Cellular Biology, January 1999, p. 136-146, Vol. 19, No. 1
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Glutamate Induces Phosphorylation of Elk-1 and CREB, Along with c-fos Activation, via an Extracellular Signal-Regulated Kinase-Dependent Pathway in Brain Slices

Peter Vanhoutte,1 Jean-Vianney Barnier,2 Bernard Guibert,2 Christiane Pagès,1 Marie-Jo Besson,1 Robert A. Hipskind,3 and Jocelyne Caboche1,*

Laboratoire de Neurochimie-Anatomie, Institut des Neurosciences-Unité Mixte de Recherche 7624, CNRS-Universtité Pierre et Marie Curie, 75005 Paris,1 Institut Alfred Fessard, Unité Propre de Recherche 2212, CNRS, 91198 Gif sur Yvette,2 and Institut de Génétique Moléculaire, Unité Mixte de Recherche 5535, Centre National de la Recherche Scientifique, 34293 Montpellier,3 France

Received 24 June 1998/Returned for modification 28 July 1998/Accepted 30 September 1998

In cell culture systems, the TCF Elk-1 represents a convergence point for extracellular signal-related kinase (ERK) and c-Jun N-terminal kinase/stress-activated protein kinase (JNK/SAPK) subclasses of mitogen-activated protein kinase (MAPK) cascades. Its phosphorylation strongly potentiates its ability to activate transcription of the c-fos promoter through a ternary complex assembled on the c-fos serum response element. In rat brain postmitotic neurons, Elk-1 is strongly expressed (V. Sgambato, P. Vanhoutte, C. Pagès, M. Rogard, R. A. Hipskind, M. J. Besson, and J. Caboche, J. Neurosci. 18:214-226, 1998). However, its physiological role in these postmitotic neurons remains to be established. To investigate biochemically the signaling pathways targeting Elk-1 and c-fos in mature neurons, we used a semi-in vivo system composed of brain slices stimulated with the excitatory neurotransmitter glutamate. Glutamate treatment leads to a robust, progressive activation of the ERK and JNK/SAPK MAPK cascades. This corresponds kinetically to a significant increase in Ser383-phosphorylated Elk-1 and the appearance of c-fos mRNA. Glutamate also causes increased levels of Ser133-phosphorylated cyclic AMP-responsive element-binding protein (CREB) but only transiently relative to Elk-1 and c-fos. ERK and Elk-1 phosphorylation are blocked by the MAPK kinase inhibitor PD98059, indicating the primary role of the ERK cascade in mediating glutamate signaling to Elk-1 in the rat striatum in vivo. Glutamate-mediated CREB phosphorylation is also inhibited by PD98059 treatment. Interestingly, KN62, which interferes with calcium-calmodulin kinase (CaM-K) activity, leads to a reduction of glutamate-induced ERK activation and of CREB phosphorylation. These data indicate that ERK functions as a common component in two signaling pathways (ERK/Elk-1 and ERK/?/CREB) converging on the c-fos promoter in postmitotic neuronal cells and that CaM-Ks act as positive regulators of these pathways.

* Corresponding author. Mailing address: Laboratoire de Neurochimie-Anatomie, Institut des Neurosciences-Unité Mixte de Recherche 7624, Université Pierre et Marie Curie, 9 quai St-Bernard, 75005 Paris, France. Phone: 33-01-44-27-25-01. Fax: 33-01-44-27-26-69. E-mail: Jocelyne.Caboche{at}snv.jussieu.fr.

Molecular and Cellular Biology, January 1999, p. 136-146, Vol. 19, No. 1
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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