Differential mechanisms of glutamate receptor regulation of SynGAP in cortical neurones |
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Authors: | Rockliffe Nichola Gawler Debra |
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Affiliation: | The Physiological laboratory, University of Liverpool, Crown Street, Liverpool L69 3BX, UK. nichola.rockliffe@liverpool.ac.uk |
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Abstract: | One prime candidate linking N-methyl-D-aspartate (NMDA) receptors to the regulation of the MAP kinase cascade is SynGAP, a negative regulator of Ras. In order to assess how a physiological stimulus can alter SynGAP activity, an appropriate whole cell system must be used and SynGAP must be specifically extracted from membranes whilst preserving the catalytic activity of the protein. Here, we have achieved this and studied the effect of NMDA/alpha-amino-3-hydroxy-5-methylisoxazole-4-propionic acid (AMPA) and kainate receptor stimulations on SynGAP activity in cortical neurones. Furthermore, we have examined the role of extracellular Ca2+, CaM kinase II and the PSD-95-NR2B subunit interaction in SynGAP activity regulation and propose a novel convergence of signalling between AMPA, kainate and NMDA receptors. |
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Keywords: | PBS, phosphate-buffered saline GAP, GTPase activating protein NMDA, N-methyl- smallcaps" >d-aspartate AMPA, α-amino-3-hydroxy-5-methylisoxazole-4-propionic acid APV, smallcaps" >d(−)-2-amino-5-phosphono-pentanoic acid SDS, sodium dodecylsulphate PSD, post synaptic density |
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