scholarly journals ADAR2-mediated Q/R editing of GluK2 regulates kainate receptor upscaling in response to suppression of synaptic activity

2018 ◽  
Vol 131 (24) ◽  
pp. jcs222273 ◽  
Author(s):  
Sonam Gurung ◽  
Ashley J. Evans ◽  
Kevin A. Wilkinson ◽  
Jeremy M. Henley
Keyword(s):  
Synaptic Activity ◽  
Kainate Receptor

Synaptic plasticity of kainate receptors

2006 ◽  
Vol 34 (5) ◽  
pp. 949-951 ◽  
Author(s):  
J.R. Mellor
Keyword(s):  
Synaptic Plasticity ◽  
Receptor Trafficking ◽  
Synaptic Activity ◽  
Kainate Receptors ◽  
Ionotropic Glutamate Receptors ◽  
Kainate Receptor ◽  
Ionotropic Glutamate Receptor ◽  
Cellular Mechanisms ◽  
The Third ◽  
Current State

Synaptic plasticity of ionotropic glutamate receptors has been extensively studied with a particular focus on the role played by NMDA (N-methyl-D-aspartate) receptors in the induction of synaptic plasticity and the subsequent movement of AMPA (α-amino-3-hydroxy-5-methylisoxazole-4-propionic acid) receptors. The third subtype of ionotropic glutamate receptor, kainate receptors, has not been studied to the same extent, but recent evidence shows that these receptors also exhibit synaptic plasticity in response to activity. There is also a growing body of data on the mechanisms underlying kainate receptor trafficking and the proteins they interact with. This review summarizes the current state of knowledge on this topic, focusing on the evidence for the removal or insertion of functional kainate receptors in response to synaptic activity and the cellular mechanisms that underlie this regulation of neuronal kainate receptor function.

scholarly journals ADAR2-mediated Q/R editing of GluK2 regulates kainate receptor upscaling in response to suppression of synaptic activity

2018 ◽  
Author(s):  
Sonam Gurung ◽  
Ashley J. Evans ◽  
Kevin A. Wilkinson ◽  
Jeremy M. Henley
Keyword(s):  
Neuronal Excitability ◽  
Proteasomal Degradation ◽  
Surface Expression ◽  
Synaptic Activity ◽  
Kainate Receptors ◽  
Kainate Receptor ◽  
Mrna Editing ◽  
Network Function ◽  
Ampar Trafficking ◽  
Editing Enzyme

AbstractKainate receptors (KARs) regulate neuronal excitability and network function. Most KARs contain the subunit GluK2 and the properties of these receptors are determined in part by ADAR2-mediated mRNA editing of GluK2 that changes a genomically encoded glutamine (Q) to arginine (R). Suppression of synaptic activity reduces ADAR2-dependent Q/R editing of GluK2 with a consequential increase in GluK2-containing KAR surface expression. However, the mechanism underlying this reduction in GluK2 editing has not been addressed. Here we show that induction of KAR upscaling results in proteasomal degradation of ADAR2, which reduces GluK2 Q/R editing. Because KARs incorporating unedited GluK2(Q) assemble and exit the ER more efficiently this leads to an upscaling of KAR surface expression. Consistent with this, we demonstrate that partial ADAR2 knockdown phenocopies and occludes KAR upscaling. Moreover, we show that although the AMPAR subunit GluA2 also undergoes ADAR2-dependent Q/R editing, this process does not mediate AMPAR upscaling. These data demonstrate that activity-dependent regulation of ADAR2 proteostasis and GluK2 Q/R editing are key determinants of KAR, but not AMPAR, trafficking and upscaling.Summary statementSynaptic suppression promotes proteasomal degradation of the mRNA-editing enzyme ADAR2. Decreased ADAR2 levels reduce Q/R editing of the kainate receptor subunit GluK2 leading to enhanced surface expression and homeostatic upscaling.

Ischemic preconditioning protects the hippocampal CA1 neurons by inhibiting synaptic activity in rat

2005 ◽  
Vol 25 (1_suppl) ◽  
pp. S300-S300
Author(s):  
Thomas J Sick ◽  
Ami P Raval ◽  
Isabel Saul ◽  
Kunjan R Dave ◽  
Raul Busto ◽  
...  
Keyword(s):  
Ischemic Preconditioning ◽  
Synaptic Activity ◽  
Ca1 Neurons ◽  
Hippocampal Ca1 Neurons ◽  
Hippocampal Ca1
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