A synaptic Ras-GTPase activating protein (p135 SynGAP) inhibited by CaM kinase II
| Autor: | Michelle Rojas-Soto, Hong Jung Chen, Mary B. Kennedy, Asako Oguni |
|---|---|
| Rok vydání: | 1998 |
| Předmět: |
Scaffold protein
GTPase-activating protein Neuroscience(all) Molecular Sequence Data Glutamic Acid SYNGAP1 Hippocampus Receptors N-Methyl-D-Aspartate GTP Phosphohydrolases Substrate Specificity Ca2+/calmodulin-dependent protein kinase Animals RNA Messenger Enzyme Inhibitors Phosphorylation Cells Cultured Neurons Sequence Homology Amino Acid Chemistry General Neuroscience GTPase-Activating Proteins Neuropeptides Glutamate receptor Brain Cell biology Rats nervous system Synaptic plasticity Calcium-Calmodulin-Dependent Protein Kinases Synapses ras Proteins NMDA receptor Calcium-Calmodulin-Dependent Protein Kinase Type 2 Carrier Proteins Postsynaptic density |
| Zdroj: | Neuron. 20(5) |
| ISSN: | 0896-6273 |
| Popis: | Ca2+ influx through N-methyl-D-aspartate– (NMDA–) type glutamate receptors plays a critical role in synaptic plasticity in the brain. One of the proteins activated by the increase in Ca2+ is CaM kinase II (CaMKII). Here, we report a novel synaptic Ras-GTPase activating protein (p135 SynGAP) that is a major component of the postsynaptic density, a complex of proteins associated with synaptic NMDA receptors. p135 SynGAP is almost exclusively localized at synapses in hippocampal neurons where it binds to and closely colocalizes with the scaffold protein PSD-95 and colocalizes with NMDA receptors. The Ras-GTPase activating activity of p135 SynGAP is inhibited by phosphorylation by CaMKII located in the PSD protein complex. Inhibition of p135 SynGAP by CaMKII will stop inactivation of GTP-bound Ras and thus could result in activation of the mitogen-activated protein (MAP) kinase pathway in hippocampal neurons upon activation of NMDA receptors. |
| Databáze: | OpenAIRE |
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