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GRIA1 Membrane Protein Introduction

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
Gene Name GRIA1
Aliases GluR-1, AMPA-selective glutamate receptor 1, GluR-A, GluR-K1, Glutamate receptor ionotropic, AMPA 1, GluA1, GLUH1, GLUR1
Organism Homo sapiens (Human)
UniProt ID P42261
Transmembrane Times 3
Length (aa) 906
Sequence MQHIFAFFCTGFLGAVVGANFPNNIQIGGLFPNQQSQEHAAFRFALSQLTEPPKLLPQIDIVNISDSFEMTYRFCSQFSKGVYAIFGFYERRTVNMLTSFCGALHVCFITPSFPVDTSNQFVLQLRPELQDALISIIDHYKWQKFVYIYDADRGLSVLQKVLDTAAEKNWQVTAVNILTTTEEGYRMLFQDLEKKKERLVVVDCESERLNAILGQIIKLEKNGIGYHYILANLGFMDIDLNKFKESGANVTGFQLVNYTDTIPAKIMQQWKNSDARDHTRVDWKRPKYTSALTYDGVKVMAEAFQSLRRQRIDISRRGNAGDCLANPAVPWGQGIDIQRALQQVRFEGLTGNVQFNEKGRRTNYTLHVIEMKHDGIRKIGYWNEDDKFVPAATDAQAGGDNSSVQNRTYIVTTILEDPYVMLKKNANQFEGNDRYEGYCVELAAEIAKHVGYSYRLEIVSDGKYGARDPDTKAWNGMVGELVYGRADVAVAPLTITLVREEVIDFSKPFMSLGISIMIKKPQKSKPGVFSFLDPLAYEIWMCIVFAYIGVSVVLFLVSRFSPYEWHSEEFEEGRDQTTSDQSNEFGIFNSLWFSLGAFMQQGCDISPRSLSGRIVGGVWWFFTLIIISSYTANLAAFLTVERMVSPIESAEDLAKQTEIAYGTLEAGSTKEFFRRSKIAVFEKMWTYMKSAEPSVFVRTTEEGMIRVRKSKGKYAYLLESTMNEYIEQRKPCDTMKVGGNLDSKGYGIATPKGSALRNPVNLAVLKLNEQGLLDKLKNKWWYDKGECGSGGGDSKDKTSALSLSNVAGVFYILIGGLGLAMLVALIEFCYKSRSESKRMKGFCLIPQQSINEAIRTSTLPRNSGAGASSGGSGENGRVVSHDFPKSMQSIPCMSHSSGMPLGATGL

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.

Physical map of GRIA1.Fig.1 Physical map of GRIA1.

Application of GRIA1 Membrane Protein in Literature

  1. Cabrera-Pastor A., et al. Chronic hyperammonemia alters in opposite ways membrane expression of GluA1 and GluA2 AMPA receptor subunits in cerebellum. Molecular mechanisms involved. Biochim Biophys Acta. 2018, 1864(1): 286-295. PubMed ID: 29107806

    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.

  2. Zhang B., et al. Src homology 2 domain-containing phosphotyrosine phosphatase 2 (Shp2) controls surface GluA1 protein in synaptic homeostasis. J Biol Chem. 2017, 292(37): 15481-15488. PubMed ID: 28768764

    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.

  3. Guntupalli S., et al. GluA1 subunit ubiquitination mediates amyloid-β-induced loss of surface α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptors. J Biol Chem. 2017, 292(20): 8186-8194. PubMed ID: 28377502

    The article indicates that the GluA1 S845D phosphomimetic mutant reduced binding with Nedd4-1 and hence the ubiquitination of AMPARs.

  4. Zhang K., et al. Essential roles of AMPA receptor GluA1 phosphorylation and presynaptic HCN channels in fast-acting antidepressant responses of ketamine. Sci Signal. 2016, 9(458): ra123. PubMed ID: 27965425

    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.

  5. He X.Y., et al. GluA1 signal peptide determines the spatial assembly of heteromeric AMPA receptors. Proc Natl Acad Sci U S A. 2016, 113(38): E5645-54. PubMed ID: 27601647

    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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