Glutamate receptors are the predominant excitatory neurotransmitter receptors in the mammalian brain and are activated in a variety of normal neurophysiologic processes. These receptors are heteromeric protein complexes with multiple subunits, each possessing transmembrane regions, and all arranged to form a ligand-gated ion channel. The classification of glutamate receptors is based on their activation by different pharmacologic agonists. This gene belongs to a family of alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate (AMPA) receptors. Alternative splicing at this locus results in several different isoforms which may vary in their signal transduction properties.[7]
Genome studies have uncovered a tentative link between defective GRIA3 variants and a highly elevated risk of schizophrenia.
Several ion channels and neurotransmitters receptors pre-mRNA as substrates for ADARs.[9] This includes 5 subunits of the glutamate receptor: ionotropic AMPA glutamate receptor subunits (GluA2, GluA3, GluA4) and kainate receptor subunits (GluK1, GluK2). Glutamate gated ion channels are made up of four subunits per channel with each subunit contributing to the pore loop structure. The pore loop structure is related to that found in K+ channels (e.g., human Kv1.1 channel).[10] The human Kv1.1 channel pre mRNA is also subject to A to I RNA editing.[11] The function of the glutamate receptors is in the mediation of fast neurotransmission to the brain. The diversity of the subunits is determined, as well as rna splicing by RNA editing events of the individual subunits. This give rise to the necessarily high diversity of these receptors. GluR3 is a gene product of the GRIA3 gene and its pre-mRNA is subject to RNA editing.
TypeEdit
A to I RNA editing is catalyzed by a family of adenosine deaminases acting on RNA (ADARs) that specifically recognize adenosines within double-stranded regions of pre-mRNAs and deaminate them to inosine. Inosines are recognised as guanosine by the cells translational machinery. There are three members of the ADAR family ADARs 1-3, with ADAR1 and ADAR2 being the only enzymatically active members. ADAR3 is thought to have a regulatory role in the brain. ADAR1 and ADAR2 are widely expressed in tissues while ADAR3 is restricted to the brain. The double-stranded regions of RNA are formed by base-pairing between residues in the close to region of the editing site with residues usually in a neighboring intron but can be an exonic sequence. The region that base pairs with the editing region is known as an Editing Complementary Sequence (ECS)
LocationEdit
The pre-mRNA of this subunit is edited at one position. The R/G editing site is located in exon 13 between the M3 and M4 regions. Editing results in a codon change from an arginine (AGA) to a glycine (GGA). The location of editing corresponds to a bipartite ligand interaction domain of the receptor. The R/G site is found at amino acid 769 immediately before the 38-amino-acid-long flip and flop modules introduced by alternative splicing. Flip and Flop forms are present in both edited and nonedited versions of this protein.[12] The editing complementary sequence (ECS) is found in an intronic sequence close to the exon. The intronic sequence includes a 5' splice site. The predicted double stranded region is 30 base pairs in length. The adenosine residue is mismatched in genomically encoded transcript, however this is not the case following editing. Despite similar sequences to the Q/R site of GluR-B, editing at this site does not occur in GluR-3 pre-mRNA. Editing results in the targeted adenosine, which is mismatched prior to editing in the double-stranded RNA structure to become matched after editing. The intronic sequence involved contains a 5' donor splice site.[12][13]
Editing of GluR-3 is regulated in rat brain from low levels in embryonic stage to a large increase in editing levels at birth. In humans, 80-90% of GRIA3 transcripts are edited.[12] The absence of the Q/R site editing in this glutamate receptor subunit is due to the absence of necessary intronic sequence required to form a duplex.[14]
ConsequencesEdit
StructureEdit
Editing results in a codon change from (AGA) to (GGA), an R to a G change at the editing site.[12]
FunctionEdit
Editing at R/G site allows for faster recovery from desensitisation. Unedited Glu-R at this site have slower recovery rates. Editing, therefore, allow sustained response to rapid stimuli. A crosstalk between editing and splicing is likely to occur here. Editing takes place before splicing. All AMPA receptors occur in flip and flop alternatively spliced variants. AMPA receptors that occur in the Flop form desenstise faster than the flip form.[12] Editing is also thought to affect splicing at this site.
^ abHirbec, Hélène; Perestenko Olga; Nishimune Atsushi; Meyer Guido; Nakanishi Shigetada; Henley Jeremy M; Dev Kumlesh K (May 2002). "The PDZ proteins PICK1, GRIP, and syntenin bind multiple glutamate receptor subtypes. Analysis of PDZ binding motifs". J. Biol. Chem. 277 (18): 15221–4. doi:10.1074/jbc.C200112200. ISSN 0021-9258. PMID 11891216.
^Bass BL (2002). "RNA editing by adenosine deaminases that act on RNA". Annu. Rev. Biochem. 71: 817–46. doi:10.1146/annurev.biochem.71.110601.135501. PMC1823043. PMID 12045112.
^Seeburg PH, Single F, Kuner T, Higuchi M, Sprengel R (July 2001). "Genetic manipulation of key determinants of ion flow in glutamate receptor channels in the mouse". Brain Res. 907 (1–2): 233–43. doi:10.1016/S0006-8993(01)02445-3. PMID 11430906. S2CID 11969068.
^Bhalla T, Rosenthal JJ, Holmgren M, Reenan R (October 2004). "Control of human potassium channel inactivation by editing of a small mRNA hairpin". Nat. Struct. Mol. Biol. 11 (10): 950–6. doi:10.1038/nsmb825. PMID 15361858. S2CID 34081059.
^ abcdefLomeli H, Mosbacher J, Melcher T, Höger T, Geiger JR, Kuner T, Monyer H, Higuchi M, Bach A, Seeburg PH (December 1994). "Control of kinetic properties of AMPA receptor channels by nuclear RNA editing". Science. 266 (5191): 1709–13. Bibcode:1994Sci...266.1709L. doi:10.1126/science.7992055. PMID 7992055.
^Seeburg PH, Higuchi M, Sprengel R (May 1998). "RNA editing of brain glutamate receptor channels: mechanism and physiology". Brain Res. Brain Res. Rev. 26 (2–3): 217–29. doi:10.1016/S0165-0173(97)00062-3. PMID 9651532. S2CID 12147763.
^Herb A, Higuchi M, Sprengel R, Seeburg PH (March 1996). "Q/R site editing in kainate receptor GluR5 and GluR6 pre-mRNAs requires distant intronic sequences". Proc. Natl. Acad. Sci. U.S.A. 93 (5): 1875–80. Bibcode:1996PNAS...93.1875H. doi:10.1073/pnas.93.5.1875. PMC39875. PMID 8700852.
Further readingEdit
Hollmann M, Hartley M, Heinemann S (1991). "Ca2+ permeability of KA-AMPA--gated glutamate receptor channels depends on subunit composition". Science. 252 (5007): 851–3. Bibcode:1991Sci...252..851H. doi:10.1126/science.1709304. PMID 1709304. S2CID 27103108.
Rampersad V, Elliott CE, Nutt SL, et al. (1994). "Human glutamate receptor hGluR3 flip and flop isoforms: cloning and sequencing of the cDNAs and primary structure of the proteins". Biochim. Biophys. Acta. 1219 (2): 563–6. doi:10.1016/0167-4781(94)90090-6. PMID 7918660.
Rogers SW, Andrews PI, Gahring LC, et al. (1994). "Autoantibodies to glutamate receptor GluR3 in Rasmussen's encephalitis". Science. 265 (5172): 648–51. Bibcode:1994Sci...265..648R. doi:10.1126/science.8036512. PMID 8036512.
Tomiyama M, Rodriguez-Puertas R, Cortés R, et al. (1997). "Differential regional distribution of AMPA receptor subunit messenger RNAs in the human spinal cord as visualized by in situ hybridization". Neuroscience. 75 (3): 901–15. doi:10.1016/0306-4522(96)00321-1. hdl:10261/112658. PMID 8951883. S2CID 20271430.
Osten P, Srivastava S, Inman GJ, et al. (1998). "The AMPA receptor GluR2 C terminus can mediate a reversible, ATP-dependent interaction with NSF and alpha- and beta-SNAPs". Neuron. 21 (1): 99–110. doi:10.1016/S0896-6273(00)80518-8. PMID 9697855.
Srivastava S, Osten P, Vilim FS, et al. (1998). "Novel anchorage of GluR2/3 to the postsynaptic density by the AMPA receptor-binding protein ABP". Neuron. 21 (3): 581–91. doi:10.1016/S0896-6273(00)80568-1. PMID 9768844.
Hayashi T, Umemori H, Mishina M, Yamamoto T (1999). "The AMPA receptor interacts with and signals through the protein tyrosine kinase Lyn". Nature. 397 (6714): 72–6. Bibcode:1999Natur.397...72H. doi:10.1038/16269. PMID 9892356. S2CID 4327273.
Amir R, Dahle EJ, Toriolo D, Zoghbi HY (2000). "Candidate gene analysis in Rett syndrome and the identification of 21 SNPs in Xq". Am. J. Med. Genet. 90 (1): 69–71. doi:10.1002/(SICI)1096-8628(20000103)90:1<69::AID-AJMG12>3.0.CO;2-W. PMID 10602120.
Aruscavage PJ, Bass BL (2000). "A phylogenetic analysis reveals an unusual sequence conservation within introns involved in RNA editing". RNA. 6 (2): 257–69. doi:10.1017/S1355838200991921. PMC1369911. PMID 10688364.
Gahring L, Carlson NG, Meyer EL, Rogers SW (2001). "Granzyme B proteolysis of a neuronal glutamate receptor generates an autoantigen and is modulated by glycosylation". J. Immunol. 166 (3): 1433–8. doi:10.4049/jimmunol.166.3.1433. PMID 11160179.
Liu QJ, Gong YQ, Chen BX, et al. (2001). "[Linkage analysis and mutation detection of GRIA3 in Smith--Fineman--Myers syndrome]". Yi Chuan Xue Bao. 28 (11): 985–90. PMID 11725645.
Hirbec H, Perestenko O, Nishimune A, et al. (2002). "The PDZ proteins PICK1, GRIP, and syntenin bind multiple glutamate receptor subtypes. Analysis of PDZ binding motifs". J. Biol. Chem. 277 (18): 15221–4. doi:10.1074/jbc.C200112200. PMID 11891216.
Wyszynski M, Kim E, Dunah AW, et al. (2002). "Interaction between GRIP and liprin-alpha/SYD2 is required for AMPA receptor targeting". Neuron. 34 (1): 39–52. doi:10.1016/S0896-6273(02)00640-2. PMID 11931740.
Tomiyama M, Rodríguez-Puertas R, Cortés R, et al. (2002). "Flip and flop splice variants of AMPA receptor subunits in the spinal cord of amyotrophic lateral sclerosis". Synapse. 45 (4): 245–9. CiteSeerX10.1.1.575.9300. doi:10.1002/syn.10098. PMID 12125045. S2CID 28604714.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC139241. PMID 12477932.
Ganor Y, Besser M, Ben-Zakay N, et al. (2003). "Human T cells express a functional ionotropic glutamate receptor GluR3, and glutamate by itself triggers integrin-mediated adhesion to laminin and fibronectin and chemotactic migration". J. Immunol. 170 (8): 4362–72. doi:10.4049/jimmunol.170.8.4362. PMID 12682273.
Flajolet M, Rakhilin S, Wang H, et al. (2004). "Protein phosphatase 2C binds selectively to and dephosphorylates metabotropic glutamate receptor 3". Proc. Natl. Acad. Sci. U.S.A. 100 (26): 16006–11. Bibcode:2003PNAS..10016006F. doi:10.1073/pnas.2136600100. PMC307683. PMID 14663150.
Kolleker A, Zhu JJ, Schupp BJ, et al. (2004). "Glutamatergic plasticity by synaptic delivery of GluR-B(long)-containing AMPA receptors". Neuron. 40 (6): 1199–212. doi:10.1016/S0896-6273(03)00722-0. PMID 14687553.
gria3, glutamate, receptor, protein, that, humans, encoded, gene, available, structurespdbortholog, search, pdbe, rcsblist, codes3lsw, 3lsxidentifiersaliases, glur, glur, glur3, glurc, glua3, mrx94, glutamate, ionotropic, receptor, ampa, type, subunit, mrxswex. Glutamate receptor 3 is a protein that in humans is encoded by the GRIA3 gene 5 6 7 GRIA3Available structuresPDBOrtholog search PDBe RCSBList of PDB id codes3LSW 3LSXIdentifiersAliasesGRIA3 GLUR C GLUR K3 GLUR3 GLURC GluA3 MRX94 glutamate ionotropic receptor AMPA type subunit 3 MRXSWExternal IDsOMIM 305915 MGI 95810 HomoloGene 37353 GeneCards GRIA3Gene location Human Chr X chromosome human 1 BandXq25Start123 184 153 bp 1 End123 490 915 bp 1 Gene location Mouse Chr X chromosome mouse 2 BandX A4 X 23 19 cMStart40 489 731 bp 2 End40 767 478 bp 2 RNA expression patternBgeeHumanMouse ortholog Top expressed inBrodmann area 23middle temporal gyrusentorhinal cortexpostcentral gyrussuperior frontal gyrusBrodmann area 9prefrontal cortexhippocampus propernucleus accumbenscingulate gyrusTop expressed insubiculumolfactory tuberclenucleus accumbenslateral geniculate nucleusfacial motor nucleusprefrontal cortexcerebellar vermisventromedial nucleusmedial geniculate nucleussuperior frontal gyrusMore reference expression dataBioGPSMore reference expression dataGene ontologyMolecular functionion channel activity ionotropic glutamate receptor activity extracellularly glutamate gated ion channel activity AMPA glutamate receptor activity excitatory extracellular ligand gated ion channel activity amyloid beta binding signaling receptor activity transmitter gated ion channel activity involved in regulation of postsynaptic membrane potentialCellular componentintegral component of membrane endocytic vesicle membrane postsynaptic membrane membrane synapse cell junction AMPA glutamate receptor complex plasma membrane parallel fiber to Purkinje cell synapseBiological processglutamate receptor signaling pathway ion transport ion transmembrane transport ionotropic glutamate receptor signaling pathway transport excitatory postsynaptic potential regulation of postsynaptic membrane potential regulation of NMDA receptor activitySources Amigo QuickGOOrthologsSpeciesHumanMouseEntrez289253623EnsemblENSG00000125675ENSMUSG00000001986UniProtP42263Q9Z2W9RefSeq mRNA NM 181894NM 000828NM 001256743NM 007325NM 001281929NM 016886NM 001290451NM 001358361RefSeq protein NP 000819NP 001243672NP 015564NP 001268858NP 001277380NP 058582NP 001345290Location UCSC Chr X 123 18 123 49 MbChr X 40 49 40 77 MbPubMed search 3 4 WikidataView Edit HumanView Edit Mouse Contents 1 Function 2 Interactions 3 RNA editing 3 1 Type 3 2 Location 3 3 Conservation 3 4 Regulation 3 5 Consequences 3 5 1 Structure 3 5 2 Function 4 See also 5 References 6 Further reading 7 External linksFunction EditGlutamate receptors are the predominant excitatory neurotransmitter receptors in the mammalian brain and are activated in a variety of normal neurophysiologic processes These receptors are heteromeric protein complexes with multiple subunits each possessing transmembrane regions and all arranged to form a ligand gated ion channel The classification of glutamate receptors is based on their activation by different pharmacologic agonists This gene belongs to a family of alpha amino 3 hydroxy 5 methyl 4 isoxazole propionate AMPA receptors Alternative splicing at this locus results in several different isoforms which may vary in their signal transduction properties 7 Genome studies have uncovered a tentative link between defective GRIA3 variants and a highly elevated risk of schizophrenia Interactions EditGRIA3 has been shown to interact with GRIP1 8 and PICK1 8 RNA editing EditSeveral ion channels and neurotransmitters receptors pre mRNA as substrates for ADARs 9 This includes 5 subunits of the glutamate receptor ionotropic AMPA glutamate receptor subunits GluA2 GluA3 GluA4 and kainate receptor subunits GluK1 GluK2 Glutamate gated ion channels are made up of four subunits per channel with each subunit contributing to the pore loop structure The pore loop structure is related to that found in K channels e g human Kv1 1 channel 10 The human Kv1 1 channel pre mRNA is also subject to A to I RNA editing 11 The function of the glutamate receptors is in the mediation of fast neurotransmission to the brain The diversity of the subunits is determined as well as rna splicing by RNA editing events of the individual subunits This give rise to the necessarily high diversity of these receptors GluR3 is a gene product of the GRIA3 gene and its pre mRNA is subject to RNA editing Type Edit A to I RNA editing is catalyzed by a family of adenosine deaminases acting on RNA ADARs that specifically recognize adenosines within double stranded regions of pre mRNAs and deaminate them to inosine Inosines are recognised as guanosine by the cells translational machinery There are three members of the ADAR family ADARs 1 3 with ADAR1 and ADAR2 being the only enzymatically active members ADAR3 is thought to have a regulatory role in the brain ADAR1 and ADAR2 are widely expressed in tissues while ADAR3 is restricted to the brain The double stranded regions of RNA are formed by base pairing between residues in the close to region of the editing site with residues usually in a neighboring intron but can be an exonic sequence The region that base pairs with the editing region is known as an Editing Complementary Sequence ECS Location Edit The pre mRNA of this subunit is edited at one position The R G editing site is located in exon 13 between the M3 and M4 regions Editing results in a codon change from an arginine AGA to a glycine GGA The location of editing corresponds to a bipartite ligand interaction domain of the receptor The R G site is found at amino acid 769 immediately before the 38 amino acid long flip and flop modules introduced by alternative splicing Flip and Flop forms are present in both edited and nonedited versions of this protein 12 The editing complementary sequence ECS is found in an intronic sequence close to the exon The intronic sequence includes a 5 splice site The predicted double stranded region is 30 base pairs in length The adenosine residue is mismatched in genomically encoded transcript however this is not the case following editing Despite similar sequences to the Q R site of GluR B editing at this site does not occur in GluR 3 pre mRNA Editing results in the targeted adenosine which is mismatched prior to editing in the double stranded RNA structure to become matched after editing The intronic sequence involved contains a 5 donor splice site 12 13 Conservation Edit Editing also occurs in rat 12 Regulation Edit Editing of GluR 3 is regulated in rat brain from low levels in embryonic stage to a large increase in editing levels at birth In humans 80 90 of GRIA3 transcripts are edited 12 The absence of the Q R site editing in this glutamate receptor subunit is due to the absence of necessary intronic sequence required to form a duplex 14 Consequences Edit Structure Edit Editing results in a codon change from AGA to GGA an R to a G change at the editing site 12 Function Edit Editing at R G site allows for faster recovery from desensitisation Unedited Glu R at this site have slower recovery rates Editing therefore allow sustained response to rapid stimuli A crosstalk between editing and splicing is likely to occur here Editing takes place before splicing All AMPA receptors occur in flip and flop alternatively spliced variants AMPA receptors that occur in the Flop form desenstise faster than the flip form 12 Editing is also thought to affect splicing at this site See also EditAMPA receptorReferences Edit a b c GRCh38 Ensembl release 89 ENSG00000125675 Ensembl May 2017 a b c GRCm38 Ensembl release 89 ENSMUSG00000001986 Ensembl May 2017 Human PubMed Reference National Center for Biotechnology Information U S National Library of Medicine Mouse PubMed Reference National Center for Biotechnology Information U S National Library of Medicine McNamara JO Eubanks JH McPherson JD Wasmuth JJ Evans GA Heinemann SF Jul 1992 Chromosomal localization of human glutamate receptor genes J Neurosci 12 7 2555 62 doi 10 1523 JNEUROSCI 12 07 02555 1992 PMC 6575855 PMID 1319477 Gecz J Barnett S Liu J Hollway G Donnelly A Eyre H Eshkevari HS Baltazar R Grunn A Nagaraja R Gilliam C Peltonen L Sutherland GR Baron M Mulley JC Mar 2000 Characterization of the human glutamate receptor subunit 3 gene GRIA3 a candidate for bipolar disorder and nonspecific X linked mental retardation Genomics 62 3 356 68 doi 10 1006 geno 1999 6032 PMID 10644433 a b Entrez Gene GRIA3 glutamate receptor ionotrophic AMPA 3 a b Hirbec Helene Perestenko Olga Nishimune Atsushi Meyer Guido Nakanishi Shigetada Henley Jeremy M Dev Kumlesh K May 2002 The PDZ proteins PICK1 GRIP and syntenin bind multiple glutamate receptor subtypes Analysis of PDZ binding motifs J Biol Chem 277 18 15221 4 doi 10 1074 jbc C200112200 ISSN 0021 9258 PMID 11891216 Bass BL 2002 RNA editing by adenosine deaminases that act on RNA Annu Rev Biochem 71 817 46 doi 10 1146 annurev biochem 71 110601 135501 PMC 1823043 PMID 12045112 Seeburg PH Single F Kuner T Higuchi M Sprengel R July 2001 Genetic manipulation of key determinants of ion flow in glutamate receptor channels in the mouse Brain Res 907 1 2 233 43 doi 10 1016 S0006 8993 01 02445 3 PMID 11430906 S2CID 11969068 Bhalla T Rosenthal JJ Holmgren M Reenan R October 2004 Control of human potassium channel inactivation by editing of a small mRNA hairpin Nat Struct Mol Biol 11 10 950 6 doi 10 1038 nsmb825 PMID 15361858 S2CID 34081059 a b c d e f Lomeli H Mosbacher J Melcher T Hoger T Geiger JR Kuner T Monyer H Higuchi M Bach A Seeburg PH December 1994 Control of kinetic properties of AMPA receptor channels by nuclear RNA editing Science 266 5191 1709 13 Bibcode 1994Sci 266 1709L doi 10 1126 science 7992055 PMID 7992055 Seeburg PH Higuchi M Sprengel R May 1998 RNA editing of brain glutamate receptor channels mechanism and physiology Brain Res Brain Res Rev 26 2 3 217 29 doi 10 1016 S0165 0173 97 00062 3 PMID 9651532 S2CID 12147763 Herb A Higuchi M Sprengel R Seeburg PH March 1996 Q R site editing in kainate receptor GluR5 and GluR6 pre mRNAs requires distant intronic sequences Proc Natl Acad Sci U S A 93 5 1875 80 Bibcode 1996PNAS 93 1875H doi 10 1073 pnas 93 5 1875 PMC 39875 PMID 8700852 Further reading EditHollmann M Hartley M Heinemann S 1991 Ca2 permeability of KA AMPA gated glutamate receptor channels depends on subunit composition Science 252 5007 851 3 Bibcode 1991Sci 252 851H doi 10 1126 science 1709304 PMID 1709304 S2CID 27103108 Rampersad V Elliott CE Nutt SL et al 1994 Human glutamate receptor hGluR3 flip and flop isoforms cloning and sequencing of the cDNAs and primary structure of the proteins Biochim Biophys Acta 1219 2 563 6 doi 10 1016 0167 4781 94 90090 6 PMID 7918660 Rogers SW Andrews PI Gahring LC et al 1994 Autoantibodies to glutamate receptor GluR3 in Rasmussen s encephalitis Science 265 5172 648 51 Bibcode 1994Sci 265 648R doi 10 1126 science 8036512 PMID 8036512 Tomiyama M Rodriguez Puertas R Cortes R et al 1997 Differential regional distribution of AMPA receptor subunit messenger RNAs in the human spinal cord as visualized by in situ hybridization Neuroscience 75 3 901 15 doi 10 1016 0306 4522 96 00321 1 hdl 10261 112658 PMID 8951883 S2CID 20271430 Osten P Srivastava S Inman GJ et al 1998 The AMPA receptor GluR2 C terminus can mediate a reversible ATP dependent interaction with NSF and alpha and beta SNAPs Neuron 21 1 99 110 doi 10 1016 S0896 6273 00 80518 8 PMID 9697855 Srivastava S Osten P Vilim FS et al 1998 Novel anchorage of GluR2 3 to the postsynaptic density by the AMPA receptor binding protein ABP Neuron 21 3 581 91 doi 10 1016 S0896 6273 00 80568 1 PMID 9768844 Hayashi T Umemori H Mishina M Yamamoto T 1999 The AMPA receptor interacts with and signals through the protein tyrosine kinase Lyn Nature 397 6714 72 6 Bibcode 1999Natur 397 72H doi 10 1038 16269 PMID 9892356 S2CID 4327273 Amir R Dahle EJ Toriolo D Zoghbi HY 2000 Candidate gene analysis in Rett syndrome and the identification of 21 SNPs in Xq Am J Med Genet 90 1 69 71 doi 10 1002 SICI 1096 8628 20000103 90 1 lt 69 AID AJMG12 gt 3 0 CO 2 W PMID 10602120 Aruscavage PJ Bass BL 2000 A phylogenetic analysis reveals an unusual sequence conservation within introns involved in RNA editing RNA 6 2 257 69 doi 10 1017 S1355838200991921 PMC 1369911 PMID 10688364 Gahring L Carlson NG Meyer EL Rogers SW 2001 Granzyme B proteolysis of a neuronal glutamate receptor generates an autoantigen and is modulated by glycosylation J Immunol 166 3 1433 8 doi 10 4049 jimmunol 166 3 1433 PMID 11160179 Liu QJ Gong YQ Chen BX et al 2001 Linkage analysis and mutation detection of GRIA3 in Smith Fineman Myers syndrome Yi Chuan Xue Bao 28 11 985 90 PMID 11725645 Hirbec H Perestenko O Nishimune A et al 2002 The PDZ proteins PICK1 GRIP and syntenin bind multiple glutamate receptor subtypes Analysis of PDZ binding motifs J Biol Chem 277 18 15221 4 doi 10 1074 jbc C200112200 PMID 11891216 Wyszynski M Kim E Dunah AW et al 2002 Interaction between GRIP and liprin alpha SYD2 is required for AMPA receptor targeting Neuron 34 1 39 52 doi 10 1016 S0896 6273 02 00640 2 PMID 11931740 Tomiyama M Rodriguez Puertas R Cortes R et al 2002 Flip and flop splice variants of AMPA receptor subunits in the spinal cord of amyotrophic lateral sclerosis Synapse 45 4 245 9 CiteSeerX 10 1 1 575 9300 doi 10 1002 syn 10098 PMID 12125045 S2CID 28604714 Strausberg RL Feingold EA Grouse LH et al 2003 Generation and initial analysis of more than 15 000 full length human and mouse cDNA sequences Proc Natl Acad Sci U S A 99 26 16899 903 Bibcode 2002PNAS 9916899M doi 10 1073 pnas 242603899 PMC 139241 PMID 12477932 Ganor Y Besser M Ben Zakay N et al 2003 Human T cells express a functional ionotropic glutamate receptor GluR3 and glutamate by itself triggers integrin mediated adhesion to laminin and fibronectin and chemotactic migration J Immunol 170 8 4362 72 doi 10 4049 jimmunol 170 8 4362 PMID 12682273 Flajolet M Rakhilin S Wang H et al 2004 Protein phosphatase 2C binds selectively to and dephosphorylates metabotropic glutamate receptor 3 Proc Natl Acad Sci U S A 100 26 16006 11 Bibcode 2003PNAS 10016006F doi 10 1073 pnas 2136600100 PMC 307683 PMID 14663150 Kolleker A Zhu JJ Schupp BJ et al 2004 Glutamatergic plasticity by synaptic delivery of GluR B long containing AMPA receptors Neuron 40 6 1199 212 doi 10 1016 S0896 6273 03 00722 0 PMID 14687553 External links EditGRIA3 protein human at the U S National Library of Medicine Medical Subject Headings MeSH DARNED http darned ucc ie Overview of all the structural information available in the PDB for UniProt Q9Z2W9 Glutamate receptor 3 at the PDBe KB This article incorporates text from the United States National Library of Medicine which is in the public domain Retrieved from https en wikipedia org w index php title GRIA3 amp oldid 1168068344, wikipedia, wiki, book, books, library,
