scholarly journals Interaction of the N-Terminal Domain of the AMPA Receptor GluR4 Subunit with the Neuronal Pentraxin NP1 Mediates GluR4 Synaptic Recruitment

Neuron ◽  
2007 ◽  
Vol 55 (1) ◽  
pp. 87-102 ◽  
Author(s):  
Gek-Ming Sia ◽  
Jean-Claude Béïque ◽  
Gavin Rumbaugh ◽  
Richard Cho ◽  
Paul F. Worley ◽  
...  
Keyword(s):  
Ampa Receptor ◽  
Terminal Domain ◽  
Neuronal Pentraxin

scholarly journals Interaction of the N-Terminal Domain of the AMPA Receptor GluR4 Subunit with the Neuronal Pentraxin NP1 Mediates GluR4 Synaptic Recruitment

Neuron ◽  
2007 ◽  
Vol 55 (3) ◽  
pp. 533 ◽  
Author(s):  
Gek-Ming Sia ◽  
Jean-Claude Béïque ◽  
Gavin Rumbaugh ◽  
Richard Cho ◽  
Paul F. Worley ◽  
...  
Keyword(s):  
Ampa Receptor ◽  
Terminal Domain ◽  
Neuronal Pentraxin

scholarly journals Long-term potentiation is independent of the C-tail of the GluA1 AMPA receptor subunit

eLife ◽  
2020 ◽  
Vol 9 ◽  
Author(s):  
Javier Díaz-Alonso ◽  
Wade Morishita ◽  
Salvatore Incontro ◽  
Jeffrey Simms ◽  
Julia Holtzman ◽  
...  
Keyword(s):  
Spatial Memory ◽  
Morris Water Maze ◽  
Ampa Receptor ◽  
Water Maze ◽  
Long Term Potentiation ◽  
Receptor Subunit ◽  
Terminal Domain ◽  
Term Potentiation ◽  
Ampa Receptor Subunit

We tested the proposal that the C-terminal domain (CTD) of the AMPAR subunit GluA1 is required for LTP. We found that a knock-in mouse lacking the CTD of GluA1 expresses normal LTP and spatial memory, assayed by the Morris water maze. Our results support a model in which LTP generates synaptic slots, which capture passively diffusing AMPARs.

Cannabidiol inhibits febrile seizure by modulating AMPA receptor kinetics through its interaction with the N-terminal domain of GluA1/GluA2

2020 ◽  
Vol 161 ◽  
pp. 105128
Author(s):  
Yongzhou Yu ◽  
Zuxiao Yang ◽  
Baohua Jin ◽  
Xia Qin ◽  
Xiaoque Zhu ◽  
...  
Keyword(s):  
Ampa Receptor ◽  
Febrile Seizure ◽  
Receptor Kinetics ◽  
Terminal Domain

scholarly journals The N-terminal Domain Modulates α-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) Receptor Desensitization

2014 ◽  
Vol 289 (19) ◽  
pp. 13197-13205 ◽  
Author(s):  
Tommi Möykkynen ◽  
Sarah K. Coleman ◽  
Artur Semenov ◽  
Kari Keinänen
Keyword(s):  
Ampa Receptor ◽  
Receptor Desensitization ◽  
Terminal Domain

scholarly journals Surface Expression of GluR-D AMPA Receptor Is Dependent on an Interaction between Its C-Terminal Domain and a 4.1 Protein

2003 ◽  
Vol 23 (3) ◽  
pp. 798-806 ◽  
Author(s):  
Sarah K. Coleman ◽  
Chunlin Cai ◽  
David G. Mottershead ◽  
Jukka-Pekka Haapalahti ◽  
Kari Keinänen
Keyword(s):  
Ampa Receptor ◽  
Surface Expression ◽  
Terminal Domain

scholarly journals α-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid (AMPA) Receptor Channels Lacking the N-terminal Domain

2002 ◽  
Vol 277 (51) ◽  
pp. 49662-49667 ◽  
Author(s):  
Arja Pasternack ◽  
Sarah K. Coleman ◽  
Annukka Jouppila ◽  
David G. Mottershead ◽  
Maria Lindfors ◽  
...  
Keyword(s):  
Cell Surface ◽  
Ligand Binding ◽  
Ampa Receptor ◽  
Protein Interactions ◽  
Ampa Receptors ◽  
Terminal Domain ◽  
Gated Channel ◽  
Surface Ligand ◽  
Amino Acid Binding ◽  
G Protein Coupled

Ionotropic glutamate receptor (iGluR) subunits contain a ∼400-residue extracellular N-terminal domain (“X domain”), which is sequence-related to bacterial amino acid-binding proteins and to class C G-protein-coupled receptors. The X domain has been implicated in the assembly, transport to the cell surface, allosteric ligand binding, and desensitization in various members of the iGluR family, but its actual role in these events is poorly characterized. We have studied the properties of homomeric α-amino-3-hydroxy-5-methylisoxazolepropionate (AMPA)-selective GluR-D glutamate receptors carrying N-terminal deletions. Our analysis indicates that, surprisingly, transport to the cell surface, ligand binding properties, agonist-triggered channel activation, rapid desensitization, and allosteric potentiation by cyclothiazide can occur normally in the complete absence of the X domain (residues 22–402). The relatively intact ligand-gated channel function of a homomeric AMPA receptor in the absence of the X domain indirectly suggests more subtle roles for this domain in AMPA receptors,e.g.in the assembly of heteromeric receptors and in synaptic protein interactions.

scholarly journals Subunit-selective N-terminal domain associations organize the formation of AMPA receptor heteromers

2011 ◽  
Vol 30 (5) ◽  
pp. 959-971 ◽  
Author(s):  
Maxim Rossmann ◽  
Madhav Sukumaran ◽  
Andrew C Penn ◽  
Dmitry B Veprintsev ◽  
M Madan Babu ◽  
...  
Keyword(s):  
Ampa Receptor ◽  
Terminal Domain ◽  
Receptor Heteromers

scholarly journals A Ligand-Binding Site in the Glua3 AMPA Receptor N-Terminal Domain Observed in Druggability Simulations and X-Ray Crystallography

2019 ◽  
Vol 116 (3) ◽  
pp. 489a
Author(s):  
Ji Young Lee ◽  
James Krieger ◽  
Beatriz Herguedas ◽  
Javier García-Nafría ◽  
Anindita Dutta ◽  
...  
Keyword(s):  
Ligand Binding ◽  
Binding Site ◽  
Ampa Receptor ◽  
Ligand Binding Site ◽  
X Ray ◽  
X Ray Crystallography ◽  
Terminal Domain
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