The Interaction between Stargazin and PSD-95 Regulates AMPA Receptor Surface Trafficking
TLDR
It is shown, using single quantum dot and FRAP imaging in live hippocampal neurons, that exchange of AMPAR by lateral diffusion between extrasynaptic and synaptic sites mostly depends on the interaction of Stargazin with PSD-95 and not upon the GluR2 AMPAR subunit C terminus.About:
This article is published in Neuron.The article was published on 2007-03-01 and is currently open access. It has received 547 citations till now. The article focuses on the topics: Postsynaptic density & AMPA receptor.read more
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Journal ArticleDOI
Glutamate Receptor Ion Channels: Structure, Regulation, and Function
Stephen F. Traynelis,Lonnie P. Wollmuth,Chris J. McBain,Frank S. Menniti,Katie M. Vance,Kevin K. Ogden,Kasper B. Hansen,Hongjie Yuan,Scott J. Myers,Raymond Dingledine +9 more
TL;DR: This review discusses International Union of Basic and Clinical Pharmacology glutamate receptor nomenclature, structure, assembly, accessory subunits, interacting proteins, gene expression and translation, post-translational modifications, agonist and antagonist pharmacology, allosteric modulation, mechanisms of gating and permeation, roles in normal physiological function, as well as the potential therapeutic use of pharmacological agents acting at glutamate receptors.
Journal ArticleDOI
Central Sensitization: A Generator of Pain Hypersensitivity by Central Neural Plasticity
TL;DR: The major triggers that initiate and maintain central sensitization in healthy individuals in response to nociceptor input and in patients with inflammatory and neuropathic pain are reviewed, emphasizing the fundamental contribution and multiple mechanisms of synaptic plasticity caused by changes in the density, nature, and properties of ionotropic and metabotropic glutamate receptors.
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The cell biology of synaptic plasticity: AMPA receptor trafficking.
TL;DR: The life cycle of AMPARs is described, from their biogenesis, through their journey to the synapse, and ultimately through their demise, and how the modulation of this process is essential for brain function is discussed.
Journal ArticleDOI
Mechanisms of CaMKII action in long-term potentiation
TL;DR: In the later stages of LTP, CaMKII has a structural role in enlarging and strengthening the synapse, and produces potentiation by phosphorylating principal and auxiliary subunits of AMPA-type glutamate receptors.
Journal ArticleDOI
Synaptic AMPA Receptor Plasticity and Behavior
TL;DR: It is argued that monitoring and manipulating synaptic AMPAR trafficking represents an attractive means to study cognitive function and dysfunction in animal models.
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.
Journal ArticleDOI
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.
Journal ArticleDOI
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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A monomeric red fluorescent protein
Robert E. Campbell,Oded Tour,Amy E. Palmer,Paul Steinbach,Geoffrey S. Baird,David A. Zacharias,Roger Y. Tsien +6 more
TL;DR: This work presents the stepwise evolution of DsRed to a dimer and then either to a genetic fusion of two copies of the protein, i.e., a tandem dimer, or to a true monomer designated mRFP1 (monomeric red fluorescent protein).
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PDZ domain proteins of synapses
Eunjoon Kim,Morgan Sheng +1 more
TL;DR: PDZ domains are protein-interaction domains that are often found in multi-domain scaffolding proteins that function in the dynamic trafficking of synaptic proteins by assembling cargo complexes for transport by molecular motors.