Interaction of the C-terminal domain of δ glutamate receptor with spectrin in the dendritic spines of cultured Purkinje cells

@article{Hirai1999InteractionOT,
  title={Interaction of the C-terminal domain of $\delta$ glutamate receptor with spectrin in the dendritic spines of cultured Purkinje cells},
  author={Hirokazu Hirai and Shinji Matsuda},
  journal={Neuroscience Research},
  year={1999},
  volume={34},
  pages={281-287}
}
Clustering of δ glutamate receptors is regulated by the actin cytoskeleton in the dendritic spines of cultured rat Purkinje cells
  • H. Hirai
  • Biology, Chemistry
    The European journal of neuroscience
  • 2000
TLDR
Results suggest that morphological changes in the actin cytoskeleton regulate the δ glutamate receptor clustering on the dendritic spines, and may affect synaptic efficacy and plasticity.
Ca2+‐dependent regulation of synaptic δ2 glutamate receptor density in cultured rat Purkinje neurons
  • H. Hirai
  • Biology
    The European journal of neuroscience
  • 2001
TLDR
The results suggest that the number of synaptic δ2 receptors is controlled by endocytosis in a synaptic activity‐ and intracellular Ca2+‐dependent way, through which synaptogenesis and synaptic plasticity in Purkinje cells might be modulated.
A New Motif Necessary and Sufficient for Stable Localization of the δ2 Glutamate Receptors at Postsynaptic Spines*
TLDR
Results indicate that the E region (more specifically, a 12-amino-acid-long segment of the E2 region) is necessary for rendering GluRδ2 resistant to endocytosis from the cell surface at the spines.
Modification of AMPA receptor clustering regulates cerebellar synaptic plasticity
  • H. Hirai
  • Biology, Chemistry
    Neuroscience Research
  • 2001
Identification of Rat EMAP, a δ-Glutamate Receptor Binding Protein
TLDR
This work isolated rat EMAP, the rat homolog of a microtubule-associated protein initially isolated and characterized in echinoderms, and found it binds to delta-glutamate receptor subunits within a 50-amino-acid segment of the delta C-terminus.
Glutamate-Receptor-Like Molecule GluRδ2 Involved in Synapse Formation at Parallel Fiber-Purkinje Neuron Synapses
  • T. Hirano
  • Biology, Chemistry
    The Cerebellum
  • 2010
TLDR
GluRδ2 plays critical roles in formation, maturation, and/or maintenance of granule neuron–Purkinje neuron synapses, and synaptogenic activity depends on an extracellular N-terminal leucine/isoleucine /valine binding protein-like domain of GluR Δ2.
The C‐terminal juxtamembrane region of the δ2 glutamate receptor controls its export from the endoplasmic reticulum
TLDR
It is proposed that GluRδ2's efficient transport to the cell surface utilizes an unknown but general ER exit mechanism, which probably works in close relation to the membrane of heterologous cells and neurons.
Drosophila α- and β-Spectrin Mutations Disrupt Presynaptic Neurotransmitter Release
TLDR
The absence of spectrins does not alter postsynaptic glutamate receptor field function or the ultrastructural localization of presynaptic vesicles, however, the subcellular localization of numerous synaptic proteins is disrupted, suggesting that the defects in Presynaptic neurotransmitter release may be attributable to inappropriate assembly, transport, or localization of proteins required for synaptic function.
Glutamate Receptor Ion Channels: Structure, Regulation, and Function
TLDR
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.
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TLDR
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