The DOI matches its Crossref record; 95 of the 95 references it cites were found in a registry or an index.
Glutamate Induces Phosphorylation of Elk-1 and CREB, Along with c -fos Activation, via an Extracellular Signal-Regulated Kinase-Dependent Pathway in Brain Slices
Open accessAbstract
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.
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Self-citationKawasaki, Y., Kohno, T., Zhuang, Z.-Y., Brenner, G. J., Wang, H., Van Der Meer, C., Befort, K., Woolf, C. J., & Ji, R.-R. (2004) · The Journal of Neuroscience · doi:10.1523/jneurosci.2396-04.2004 · Cited by 386
Metadata
- Authors
- Vanhoutte, P., Barnier, J.-V., Guibert, B., Pagès, C., Besson, M.-J., Hipskind, R. A., & Caboche, J.
- Venue
- Molecular and Cellular Biology
- Publisher
- Informa UK Limited
- Published
- 1999-01-01
- Volume
- 19
- Issue
- 1
- Pages
- 136-146
- ISSN
- 0270-7306 (ISSN-L)
- 1098-5549
- OpenAlex
- W2138435646
- Cited by
- 323
- References
- 95
- FWCI
- 8.70
- Type
- journal article
- Language
- en
- Open access
- green
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- Vanhoutte, P., Barnier, J.-V., Guibert, B., Pagès, C., Besson, M.-J., Hipskind, R. A., & Caboche, J. (1999). Glutamate Induces Phosphorylation of Elk-1 and CREB, Along with c -fos Activation, via an Extracellular Signal-Regulated Kinase-Dependent Pathway in Brain Slices. Molecular and Cellular Biology. https://doi.org/10.1128/mcb.19.1.136
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