GluA2 | Ionotropic glutamate receptors | IUPHAR/BPS Guide to PHARMACOLOGY

GluA2

Target id: 445

Nomenclature: GluA2

Family: Ionotropic glutamate receptors

Annotation status:  image of a green circle Annotated and expert reviewed. Please contact us if you can help with updates.  » Email us

   GtoImmuPdb view: OFF :     Currently no data for GluA2 in GtoImmuPdb

Gene and Protein Information
Species TM P Loops AA Chromosomal Location Gene Symbol Gene Name Reference
Human 3 1 883 4q32-q33 GRIA2 glutamate ionotropic receptor AMPA type subunit 2 43,63
Mouse 3 1 883 3 E3 Gria2 glutamate receptor, ionotropic, AMPA2 (alpha 2) 55
Rat 3 1 883 2q33 Gria2 glutamate ionotropic receptor AMPA type subunit 2 6,32,47,60
Previous and Unofficial Names
GluR2 | GluRB | HBGR2 | AMPA-selective glutamate receptor 2 | glutamate receptor
Database Links
ChEMBL Target
Ensembl Gene
Entrez Gene
Human Protein Atlas
KEGG Gene
OMIM
RefSeq Nucleotide
RefSeq Protein
UniProtKB
Wikipedia
Selected 3D Structures
Image of receptor 3D structure from RCSB PDB
Description:  AMPA subtype ionotropic glutamate receptor in complex with competitive antagonist ZK 200775
PDB Id:  3KG2
Ligand:  fanapanel
Resolution:  3.55Å
Species:  Rat
References:  59
Image of receptor 3D structure from RCSB PDB
Description:  Isolated ligand binding domain dimer of GluA2 ionotropic glutamate receptor in complex with glutamate, LY 404187 and ZK 200775
PDB Id:  3KGC
Ligand:  LY404187
Resolution:  1.55Å
Species:  Rat
References:  59
Image of receptor 3D structure from RCSB PDB
Description:  Electron density map of GluA2em in complex with quisqualate and LY451646
PDB Id:  4UQK
Ligand:  quisqualate
Resolution:  0.0Å
Species:  Rat
References:  44
Natural/Endogenous Ligands
L-glutamic acid

Download all structure-activity data for this target as a CSV file

Agonists
Key to terms and symbols View all chemical structures Click column headers to sort
Ligand Sp. Action Affinity Units Reference
(S)-5-fluorowillardiine Hs Full agonist - -
[3H]AMPA Hs Full agonist - -
AMPA Hs Full agonist - -
Antagonists
Key to terms and symbols View all chemical structures Click column headers to sort
Ligand Sp. Action Affinity Units Reference
talampanel Rn Antagonist 7.5 – 7.8 pKi 70
pKi 7.5 – 7.8 (Ki 3x10-8 – 1.5x10-8 M) [70]
[3H]CNQX Hs Antagonist - -
ATPO Hs Antagonist - -
GYKI53655 Hs Antagonist - -
GYKI53784 Hs Antagonist - -
active isomer, non-competitive
tezampanel Hs Antagonist - -
NBQX Hs Antagonist - -
View species-specific antagonist tables
Channel Blockers
Key to terms and symbols View all chemical structures Click column headers to sort
Ligand Sp. Action Use-dependent Affinity Units Concentration range (M) Voltage-dependent (mV) Reference
extracellular argiotoxin Hs - no - - - no

Not voltage dependent
Channel Blocker Comments
GluA2 is also blocked by intracellular polyamines.
Allosteric Modulators
Key to terms and symbols View all chemical structures Click column headers to sort
Ligand Sp. Action Affinity Units Concentration range (M) Voltage-dependent (mV) Reference
LY404187 Hs Positive 6.8 pEC50 - no 45
pEC50 6.8 (EC50 1.5x10-7 M) [45]
Not voltage dependent
LY392098 Hs Positive 6.7 pEC50 - no 45
pEC50 6.7 (EC50 2.2x10-7 M) [45]
Not voltage dependent
cyclothiazide Hs Positive 5.7 pEC50 - no 45
pEC50 5.7 (EC50 2.24x10-6 M) [45]
Not voltage dependent
aniracetam Hs Positive - - - no

Not voltage dependent
CX516 Hs Positive - - - no

Not voltage dependent
CX546 Hs Positive - - - no

Not voltage dependent
IDRA-21 Hs Positive - - - no

Not voltage dependent
LY503430 Hs Positive - - - no

Not voltage dependent
piracetam Hs Positive - - - no

Not voltage dependent
S18986 Hs Positive - - - no

Not voltage dependent
Allosteric Modulator Comments
Piracetam and aniracetam are examples of pyrrolidinones. Cyclothiazide, S18986, and IDRA-21 are examples of benzothiadiazides. CX516 and CX546 are examples of benzylpiperidines. LY392098, LY404187 and LY503430 are examples of biarylpropylsulfonamides.
Tissue Distribution
Retina
Species:  Human
Technique:  Immunohistochemistry
References:  56
Skin
Species:  Human
Technique:  PCR, Western Blotting
References:  67
Thalamus
Species:  Human
Technique:  Quantitative PCR
References:  19
Cortex, white matter
Species:  Human
Technique:  Immunohistochemistry
References:  66
Medial temporal lobe (hippocampus, entorhinal cortex, perirhinal cortex)
Species:  Human
Technique:  In situ hybridisation
References:  4
Dorsolateral prefrontal cortex
Species:  Human
Technique:  Quantitative RT-PCR.
References:  20
Occipital cortex
Species:  Human
Technique:  Immunohistochemistry
References:  20
Spinal cord
Species:  Human
Technique:  Quantitative RT-PCR with laser capture microdissection
References:  31
Basal forebrain
Species:  Mouse
Technique:  Immunohistochemistry
References:  74
Spinal cord
Species:  Mouse
Technique:  Immunohistochemistry
References:  7-9,49
Vestibular and spiral ganglia
Species:  Mouse
Technique:  Immunohistochemistry
References:  50
Hippocampus
Species:  Mouse
Technique:  Immunohistochemistry
References:  57,73
Substantia nigra
Species:  Mouse
Technique:  Immunohistochemistry
References:  71
Cerebellum, cerebral cortex, cerebral white matter, spinal cord
Species:  Rat
Technique:  Quantitative RT-PCR with laser capture microdissection
References:  62
Lateral amygdala
Species:  Rat
Technique:  Electron microscopy
References:  51
Nucleus tractus solitarii
Species:  Rat
Technique:  Immunohistochemistry
References:  1,36-37
Medulla oblongata
Species:  Rat
Technique:  Immunohistochemistry
References:  15
Cortex, white matter
Species:  Rat
Technique:  Immunohistochemistry
References:  65
Cerebellum
Species:  Rat
Technique:  Immunohistochemistry
References:  18
Neostriatum
Species:  Rat
Technique:  Electron microscopy
References:  21
Motor nucleus
Species:  Rat
Technique:  Immunohistochemistry, electron microscopy
References:  52
Brain stem nuclei
Species:  Rat
Technique:  Immunohistochemistry
References:  38
Pineal gland
Species:  Rat
Technique:  Immunohistochemistry
References:  30
Bone
Species:  Rat
Technique:  Immunohistochemistry
References:  64
Striatum
Species:  Rat
Technique:  Immunohistochemistry
References:  16
Hippocampus
Species:  Rat
Technique:  Immunohistochemistry
References:  24
Trigeminal ganglia
Species:  Rat
Technique:  Immunohistochemistry
References:  14
Vestibular nucleus
Species:  Rat
Technique:  Immunohistochemistry
References:  69
Basolateral amygdala
Species:  Rat
Technique:  Immunohistochemistry
References:  24
Spinal cord
Species:  Rat
Technique:  Electron microscopy
References:  2,40-41
Hippocampus
Species:  Rat
Technique:  in situ hybridization.
References:  53
Olfactory bulb
Species:  Rat
Technique:  RT-PCR
References:  25
Retina
Species:  Rat
Technique:  Immunohistochemistry
References:  17,29,58
Spinal cord
Species:  Rat
Technique:  Immunohistochemistry
References:  7-8,40-41,49,68
Ventral cochlear nucleus
Species:  Rat
Technique:  Immunohistochemistry
References:  42
Dorsal cochlear nucleus
Species:  Rat
Technique:  Electron microscopy
References:  54
Dentate gyrus (hippocampus)
Species:  Rat
Technique:  Electron microscopy
References:  22,48
Inferior olive
Species:  Rat
Technique:  Immunohistochemistry
References:  13
Inferior salivatory nucleus
Species:  Rat
Technique:  Immunohistochemistry
References:  33
Dorsal root ganglion
Species:  Rat
Technique:  Immunohistochemistry
References:  72
Central cervical nucleus
Species:  Rat
Technique:  Immunohistochemistry, electron microscopy
References:  52
Geniculate ganglion
Species:  Rat
Technique:  Immunohistochemistry
References:  12
Physiological Consequences of Altering Gene Expression
Induction of seizure and death by 3 weeks in mice harbouring a Q/R site editing-incompetent GluA2 allele ( C57BL/6 mice)
Species:  Mouse
Tissue: 
Technique:  targeting of intron 11 of GluA2 gene in mouse embryonic stem cells for replacement of the ECS element by loxP
References:  10
Biologically Significant Variants
Type:  Splice variant
Species:  Rat
Description:  ‘flip’ isoform
Amino acids:  883
Nucleotide accession: 
Protein accession: 
References:  6,32,47,60
Type:  Splice variant
Species:  Human
Description:  ‘flip’ isoform
Amino acids:  883
Nucleotide accession: 
Protein accession: 
References:  32,43,63
Type:  Splice variant
Species:  Human
Description:  ‘flop’ isoform
Amino acids:  883
Nucleotide accession: 
Protein accession: 
References:  32,43,63
Type:  Splice variant
Species:  Rat
Description:  ‘flop’ isoform
Amino acids:  883
Nucleotide accession: 
Protein accession: 
References:  6,32,47,60
Type:  Splice variant
Species:  Mouse
Description:  GluA2 (short)
Amino acids:  767
Nucleotide accession: 
Protein accession: 
References:  35
Type:  Splice variant
Species:  Mouse
Description:  ’flip’ isoform (long)
Amino acids:  883
Nucleotide accession: 
Protein accession: 
References:  35,55
Type:  Splice variant
Species:  Mouse
Description:  ‘flop’ isoform (long)
Amino acids:  883
Nucleotide accession: 
Protein accession: 
References:  35,55
Biologically Significant Variant Comments
Structure: a GluA2 subunit consists of 1 extracellular N-terminal domain, 1 ligand binding domain (S1 (a domain of the N-terminal region) + S2 (a domain of the extracellular loop between M3 and M4)), 3 membrane-spanning domains (M1, M3, M4), 1 cytoplasmic re-entrant loop (M2) and 1 C-terminal intracellular domain. GluA2 exists as several splice variants: 2 C-terminal splice variants: a minor one with a long C-terminal domain (GluA2L) and the predominant variant with a short C-terminal domain. GluA2 exists as alternatively spliced ‘flip’ and ‘flop’ isoforms which differ with respect to a cassette of 35 amino acids in the extracellular loop between M3 and M4 [32,60]. Tetrameric receptors assembled from the ‘flip’ isoform enter the desensitized state more slowly, and recover more quickly, than those formed from the ‘flop’ isoform [34,46,60]. In addition, RNA editing by adenosine deaminase type 2 (CAG->CIG), which occurs in virtually all GluA2 subunits, changes residue 607 within the channel pore from glutamine to arginine (at the ‘Q/R site’) [61]. GluA1, GluA3 and GluA4 are not subject to this form of editing and thus retain glutamine at the Q/R site. AMPA receptors that lack edited GluA2 subunits are (i) of relatively high single channel conductance [5]; (ii) permeable to Ca2+ [11,26], (iii) blocked by intracellular polyamines, causing inward rectification at depolarized potentials and (iv) blocked by extracellular argiotoxin and Joro spider toxins [27]. Q/R editing also influences the oligomerisation and trafficking of GluA2 subunits [23]. RNA editing (AGA->IGA) also occurs at a codon for arginine (unedited), or glycine (edited) at a locus with the extracellular loop that immediately precedes the alternatively spliced ‘flip’ and ‘flop’ modules. Edited channels recover from desensitization at a faster rate than those that are unedited [39]. GluA2 may express with long, or short, C-termini as a consequence of alternative splicing, the short form is predominant in mouse brain [35].
General Comments
For general reviews please see:[3,28]

References

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21. Fujiyama F, Kuramoto E, Okamoto K, Hioki H, Furuta T, Zhou L, Nomura S, Kaneko T. (2004) Presynaptic localization of an AMPA-type glutamate receptor in corticostriatal and thalamostriatal axon terminals. Eur. J. Neurosci., 20 (12): 3322-30. [PMID:15610164]

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27. Iino M, Koike M, Isa T, Ozawa S. (1996) Voltage-dependent blockage of Ca(2+)-permeable AMPA receptors by joro spider toxin in cultured rat hippocampal neurones. J. Physiol. (Lond.), 496 ( Pt 2): 431-7. [PMID:8910227]

28. Isaac JT, Ashby M, McBain CJ. (2007) The role of the GluR2 subunit in AMPA receptor function and synaptic plasticity. Neuron, 54 (6): 859-71. [PMID:17582328]

29. Kamphuis W, Klooster J, Dijk F. (2003) Expression of AMPA-type glutamate receptor subunit (GluR2) in ON-bipolar neurons in the rat retina. J. Comp. Neurol., 455 (2): 172-86. [PMID:12454983]

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31. Kawahara Y, Kwak S, Sun H, Ito K, Hashida H, Aizawa H, Jeong SY, Kanazawa I. (2003) Human spinal motoneurons express low relative abundance of GluR2 mRNA: an implication for excitotoxicity in ALS. J. Neurochem., 85 (3): 680-9. [PMID:12694394]

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56. Santiago AR, Hughes JM, Kamphuis W, Schlingemann RO, Ambrósio AF. (2008) Diabetes changes ionotropic glutamate receptor subunit expression level in the human retina. Brain Res., 1198: 153-9. [PMID:18258217]

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John A. Peters, Stephane Peineau, Graham L Collingridge.
Ionotropic glutamate receptors: GluA2. Last modified on 15/07/2015. Accessed on 14/11/2018. IUPHAR/BPS Guide to PHARMACOLOGY, http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=445.