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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AMPA receptors in the synapse turnover by monomer diffusion
Jyoji Morise,Kenichi G. N. Suzuki,Kenichi G. N. Suzuki,Ayaka Kitagawa,Yoshihiko Wakazono,Kogo Takamiya,Taka A. Tsunoyama,Yuri L. Nemoto,Hiromu Takematsu,Hiromu Takematsu,Akihiro Kusumi,Akihiro Kusumi,Shogo Oka +12 more
TL;DR: It is demonstrated that AMPAR tetramers are not stable entities and readily fall apart to dimers and monomers that could reform to tetramer at the synapse, and that rapidly diffusing monomers in the plasma membrane are primarily responsible for the AMPAR turnover in the synapses.
Journal ArticleDOI
Modulation of ionotropic glutamate receptor function by vertebrate galectins
TL;DR: It is proposed that brain‐expressed galectins are potential endogenous modulators of neuronal glutamate receptors, which may play important roles in diseases of altered cellular excitability, such as epilepsy or chronic pain.
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N-glycosylation of the AMPA-type glutamate receptor regulates cell surface expression and tetramer formation affecting channel function
Munal Babu Kandel,Saki Yamamoto,Ryosuke Midorikawa,Jyoji Morise,Yoshihiko Wakazono,Shogo Oka,Kogo Takamiya +6 more
TL;DR: Data suggest that site‐specific N‐glycans on GluA1 subunit regulates tetramer formation, intracellular trafficking, and cell surface expression of AMPA‐R.
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GSG1L regulates the strength of AMPA receptor-mediated synaptic transmission but not AMPA receptor kinetics in hippocampal dentate granule neurons.
Xia Mao,Xinglong Gu,Wei Lu +2 more
TL;DR: It is found that GSG1L is important for the regulation of synaptic strength but is not critical for the modulation of AMPAR deactivation and desensitization kinetics in hippocampal dentate granule cells.
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Synaptic Changes in AMPA Receptor Subunit Expression in Cortical Parvalbumin Interneurons in the Stargazer Model of Absence Epilepsy
TL;DR: Loss of AMPAR GluA1–4 subunits in the somatosensory cortex of stargazers compared to non-epileptic control mice indicates a loss of synaptic AMPAR-mediated excitation of cortical PV+ inhibitory 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.