Received for publication July 28, 2004.
Revised December 21, 2004.
Accepted for publication December 21, 2004.

NMDA and BDNF induce distinct profiles of Extracellular regulated kinase (ERK), Mitogen and stress activated kinase (MSK) and Ribosomal S6 kinase (RSK) phosphorylation in cortical neurones

Abstract

Stimulation of NMDA receptors is thought to underly long-term memory formation and excessive NMDA receptor activation has been linked to several neuropathological conditions. Phosphorylation and activation of p42/44 MAP kinase (ERK) is believed to mediate many of these effects, but the downstream targets of ERK in response to NMDA activation have not been determined. In primary cultures of rat cortical neurones, we found that NMDA was able to elevate phosphorylation of MSK1 as well as ERK. Similarly BDNF treatment increased phosphorylation of MSK1 and ERKs. The NMDA induced MSK1 phosphorylation was sensitive to the MEK inhibitor PD98059 and the p38 inhibitor SB20350. MSK1 activation by NMDA was transient, although ERK remained phosphorylated within the neuronal cytoplasm for several hours. Whereas BDNF increased RSK phosphorylation, NMDA had no discernable effect on the phosphorylation of RSKs. Thus phosphorylation and activation of MSK1 but not RSK, could be an important step in the pathway linking NMDA induced ERK phosphorylation to the activation of transcription factors required for formation of long term memory

Key words: Glutamate, Protein Kinases (other), MAP Kinase

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