The Journal of Neuroscience, December 1, 2004, ():
A Novel Ca2+-Independent Signaling Pathway to Extracellular Signal-Regulated Protein Kinase by Coactivation of NMDA Receptors and Metabotropic Glutamate Receptor 5 in Neurons
J. Neurosci. Yang et al.
24: 10846
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Fig. 1. A schematic diagram illustrating a Ca2+-independent signaling pathway to the Ras-MAPK cascade following co-activation of N-methyl-D-aspartate receptor (NMDAR) and metabotropic glutamate receptor 5 (mGluR5) in neurons. Co-stimulation of NMDAR and mGluR5 cooperatively activates the Ras-MAPK cascade through the NMDAR-associated postsynaptic density-95 (PSD-95) and the mGluR5-associated Homer1b/c. This pathway is independent on the NMDAR-mediated Ca2+-influx and the mGluR5-mediated intracellular Ca2+ release through a G-protein/PLC/IP3 pathway. Activated MAPK/ERK possesses the ability to phosphorylate the nuclear transcription factors (Elk-1 and CREB) and thus facilitates c-Fos expression. Other abbreviations: CREB, cAMP response element-binding protein; IP3, inositol-1,4,5-triphosphate; MAPK, mitogen-activated protein kinase; PI, phosphoinositide; PLC, phospholipase C.
