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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Corticosteroid effects on glutamatergic transmission and fear memory
TL;DR: It is reported that corticosteroid hormones regulate the function, mobility, and expression of AMPA receptors, and retention ofAMPA receptors at synapses is critical for the memory enhancing effects of stress, and it is found that cortiosteroid hormone enhance the function of NMDA receptors.
Journal ArticleDOI
Long-term potentiation and spatial memory training stimulate the hippocampal expression of RyR2 calcium release channels
Ismael Valdés-Undurraga,Pedro Lobos,Virginia Sánchez-Robledo,Alejandra Arias-Cavieres,Carol D. SanMartín,Genaro Barrientos,Jamileth More,Pablo Muñoz,Andrea C. Paula-Lima,Cecilia Hidalgo,Tatiana Adasme +10 more
TL;DR: In this paper , it was shown that the increments in the protein content of RyR2 Ca2+ release channels, induced by LTP or spatial memory training, play a significant role in hippocampal synaptic plasticity and spatial memory consolidation.
Book ChapterDOI
AMPA receptor trafficking in the developing and mature glutamatergic synapse
TL;DR: An overview of the molecular mechanisms that govern the assembly, intracellular trafficking, and targeting to synapses of AMPA receptors have been uncovered are provided.
Journal ArticleDOI
NMDA and AMPA receptor physiology and role in visceral hypersensitivity: a review
TL;DR: The updated findings on the physiology of NMDARs and AMPARs and their relation to visceral hypersensitivity are reviewed and directions for future research in this field with evolving importance are proposed.
Journal ArticleDOI
GluA3 subunits are required for appropriate assembly of AMPAR GluA2 and GluA4 subunits on cochlear afferent synapses and for presynaptic ribbon modiolar–pillar morphology
TL;DR: In this paper , a 5-week-old male C57BL/6J Gria3-knockout mice (i.e., subunit GluA3KO) were determined cochlear function, synapse ultrastructure, and AMPAR molecular anatomy at ribbon synapses between inner hair cells and spiral ganglion neurons.
References
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Journal Article
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.