Subunit Composition of Synaptic AMPA Receptors Revealed by a Single-Cell Genetic Approach
Wei Lu,Yun Shi,Alexander C. Jackson,Kirsten Bjorgan,Matthew J. During,Rolf Sprengel,Peter H. Seeburg,Roger A. Nicoll +7 more
TLDR
A functional quantification of the subunit composition of AMPARs in the CNS is provided and novel roles for AMPAR subunits in receptor trafficking are suggested and suggested.About:
This article is published in Neuron.The article was published on 2009-04-30 and is currently open access. It has received 605 citations till now. The article focuses on the topics: Silent synapse & Long-term depression.read more
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Ca2+-permeable AMPA receptors in homeostatic synaptic plasticity
TL;DR: This review will summarize how synaptic expression of CP-AMPARs is regulated during homeostatic synaptic plasticity in the context of synaptic scaling, and will address the potential functional consequences of altering synaptic CP-ampAR content.
Journal ArticleDOI
Coexpressed Auxiliary Subunits Exhibit Distinct Modulatory Profiles on AMPA Receptor Function
Konstantin Khodosevich,Eric Jacobi,Eric Jacobi,Paul Farrow,Paul Farrow,Anton Schulmann,Alexandru Rusu,Ling Zhang,Rolf Sprengel,Hannah Monyer,Jakob von Engelhardt,Jakob von Engelhardt +11 more
TL;DR: Electrophysiological and biochemical evidence support the notion that CKAMP44 and TARP γ-8 can be contained in the same AMPAR complex.
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Probing TARP Modulation of AMPA Receptor Conductance with Polyamine Toxins
Alexander C. Jackson,Aaron D. Milstein,Aaron D. Milstein,David Soto,Mark Farrant,Stuart G. Cull-Candy,Roger A. Nicoll +6 more
TL;DR: The data indicate that channel block by polyamine toxins is sensitive to the mean channel conductance of AMPARs, which varies with TARP subtype and agonist efficacy, and suggest the possibility that TARPs may influence their channel properties by selectively stabilizing specific channel conformations, rather than altering the pore structure.
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GSG1L suppresses AMPA receptor-mediated synaptic transmission and uniquely modulates AMPA receptor kinetics in hippocampal neurons.
Xinglong Gu,Xia Mao,Marc P. Lussier,Mary Anne Hutchison,Liang Zhou,F. Kent Hamra,Katherine W. Roche,Wei Lu +7 more
TL;DR: GSG1L represents a new class of auxiliary subunit with distinct functional properties for AMPARs, and speeds up AMPAR deactivation and desensitization in hippocampal CA1 neurons, in contrast to the effects of TARPs and CNIHs.
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Assembly of AMPA receptors: mechanisms and regulation
TL;DR: It is proposed that this core AMPAR assembly process could be regulated by neuronal signals and speculate on possible mechanisms for such regulation.
References
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The glutamate receptor ion channels
TL;DR: The cloning of cDNAs encoding glutamate receptor subunits, which occurred mainly between 1989 and 1992, stimulated the development of ionotropic glutamate receptors in the brain.
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Cloned Glutamate Receptors
TL;DR: The application of molecular cloning technology to the study of the glutamate receptor system has led to an explosion of knowledge about the structure, expression, and function of this most important fast excitatory transmitter system in the mammalian brain.
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AMPA Receptor Trafficking and Synaptic Plasticity
TL;DR: The growing literature that supports a critical role for AMPA receptors trafficking in LTP and LTD is reviewed, focusing on the roles proposed for specific AMPA receptor subunits and their interacting proteins.
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Driving AMPA Receptors into Synapses by LTP and CaMKII: Requirement for GluR1 and PDZ Domain Interaction
Yasunori Hayashi,Song-Hai Shi,José A. Esteban,Antonella Piccini,Jean Christophe Poncer,Roberto Malinow +5 more
TL;DR: Results show that LTP and CaMKII activity drive AMPA-Rs to synapses by a mechanism that requires the association between GluR1 and a PDZ domain protein.
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RNA editing in brain controls a determinant of ion flow in glutamate-gated channels.
TL;DR: It is shown that the genomic DNA sequences encoding the particular channel segment of all subunits harbor a glutamine codon (CAG), even though an arginine codon is found in mRNAs of three subunits.