The NMDA receptor is coupled to the ERK pathway by a direct interaction between NR2B and RasGRF1
| Autor: | Roman Tyzio, Igor Medina, Yehezkel Ben-Ari, Christophe Pellegrino, Grigory Krapivinsky, Luba Krapivinsky, Anton Ivanov, Yunona Manasian, David E. Clapham |
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| Přispěvatelé: | Howard Hughes Medical Institute Children's Hospital, Epilepsie et ischémie cérébrale, Université de la Méditerranée - Aix-Marseille 2-Institut National de la Santé et de la Recherche Médicale (INSERM), Tyzio, Roman |
| Rok vydání: | 2003 |
| Předmět: |
MESH: Signal Transduction
MAPK/ERK pathway MESH: Hippocampus Hippocampus Synaptic Transmission MESH: Animals Newborn MESH: Synapses MESH: Protein Structure Tertiary MESH: Animals MESH: Neuronal Plasticity Receptor Cells Cultured Neuronal Plasticity MESH: Peptides Kinase musculoskeletal neural and ocular physiology General Neuroscience Glutamate receptor MESH: ras-GRF1 Cell biology MESH: N-Methylaspartate Excitatory postsynaptic potential NMDA receptor Signal transduction Mitogen-Activated Protein Kinases psychological phenomena and processes MESH: Cells Cultured Signal Transduction MESH: Mutation N-Methylaspartate MESH: Rats Neuroscience(all) [SDV.BC]Life Sciences [q-bio]/Cellular Biology Biology MESH: Calcium Signaling Receptors N-Methyl-D-Aspartate Fetus Organ Culture Techniques MESH: Synaptic Transmission Animals Humans Calcium Signaling [SDV.BC] Life Sciences [q-bio]/Cellular Biology MESH: Receptors N-Methyl-D-Aspartate MESH: Humans Binding Sites ras-GRF1 MESH: Fetus MESH: Mitogen-Activated Protein Kinases MESH: Organ Culture Techniques Protein Structure Tertiary Rats MESH: Binding Sites nervous system Animals Newborn Synaptic plasticity Mutation Synapses Peptides Neuroscience |
| Zdroj: | Neuron Neuron, Elsevier, 2003, 40 (4), pp.775-84 |
| ISSN: | 0896-6273 |
| Popis: | International audience; The NMDA subtype of glutamate receptors (NMDAR) at excitatory neuronal synapses plays a key role in synaptic plasticity. The extracellular signal-regulated kinase (ERK1,2 or ERK) pathway is an essential component of NMDAR signal transduction controlling the neuroplasticity underlying memory processes, neuronal development, and refinement of synaptic connections. Here we show that NR2B, but not NR2A or NR1 subunits of the NMDAR, interacts in vivo and in vitro with RasGRF1, a Ca(2+)/calmodulin-dependent Ras-guanine-nucleotide-releasing factor. Specific disruption of this interaction in living neurons abrogates NMDAR-dependent ERK activation. Thus, RasGRF1 serves as NMDAR-dependent regulator of the ERK kinase pathway. The specific association of RasGRF1 with the NR2B subunit and study of ERK activation in neurons with varied content of NR2B suggests that NR2B-containing channels are the dominant activators of the NMDA-dependent ERK pathway. |
| Databáze: | OpenAIRE |
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