Introduction of GRIA1
Glutamate receptor 1 (GRIA1), also known as AMPA-selective glutamate receptor 1 and Glutamate receptor ionotropic, is a protein that in humans is encoded by the GRIA1 gene. Glutamate receptor 1 is a member of the glutamate receptor family, which are the major excitatory neurotransmitter receptors in the mammalian brain. These receptor proteins are heteromeric protein complexes with multiple subunits. Each of them has transmembrane regions, and all are arranged to form a ligand-gated ion channel. Glutamate receptors are activated in different normal neurophysiologic processes and the classification of them is based on their activation by different pharmacologic agonists. The GRIA1 belongs to a family of alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate (AMPA) receptors. Each member (GRIA 1-4) includes flip and flop isoforms generated by alternative RNA splicing. The signal transduction properties of the receptor subunits encoded by each isoform are different. The isoform presented here is the flop isoform. Human GRIA1 mRNA is shown to present in granule and pyramidal cells in the hippocampal formation of the in situ hybridization experiments.
|Basic Information of GRIA1|
|Protein Name||Glutamate receptor 1|
|Aliases||GluR-1, AMPA-selective glutamate receptor 1, GluR-A, GluR-K1, Glutamate receptor ionotropic, AMPA 1, GluA1, GLUH1, GLUR1|
|Organism||Homo sapiens (Human)|
Function of GRIA1 Membrane Protein
AMPA receptors mediate rapid excitatory synaptic transmission and play a role in hippocampal synaptic long-term potentiation and depression. L-glutamate acts as an excitatory neurotransmitter in many synapses of the central nervous system. The binding of the excitatory neurotransmitter L-glutamate induces a conformation change that results in the opening of the cation channel, thereby converting the chemical signal into an electrical impulse. The receptor then rapidly desensitizes and enters a transient inactive state characterized by the presence of bound agonist. In the presence of CACNG4 or CACNG7 or CACNG8, it exhibits resensitization characterized by a delayed accumulation of current flux upon continued application of glutamate. Several diseases are associated with GRIA1, such as status epilepticus and fragile x syndrome.
Fig.1 Physical map of GRIA1.
Application of GRIA1 Membrane Protein in Literature
This article reveals that chronic hyperammonemia alters membrane expression of GluA1 and GluA2 AMPA receptor subunits in cerebellum in opposite ways, which leads to cognitive and motor alterations in hyperammonemia and hepatic encephalopathy.
Authors in this group demonstrate that during synaptic scaling, Shp2 phosphatase activity is essential for the regulation of Ser(P)845 GluA1 and surface expression of AMPA receptor subunit.
The article indicates that the GluA1 S845D phosphomimetic mutant reduced binding with Nedd4-1 and hence the ubiquitination of AMPARs.
The article reports that GluA1 phosphorylation and presynaptic HCN channels play a key role in fast-acting antidepressant responses of ketamine. The results provide a mechanism for changes in synaptic activity.
This article reveals the spatial assembly of an important class of glutamate receptors in the brain (GluA1), revealing a new function of signal peptides.
GRIA1 Preparation Options
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