A family of AMPA-selective glutamate receptors.

true 1991-02-01 2008-07-22 108 GRIA2_RAT GLRB_RAT GLR2_RAT Glutamate receptor 2 GluR-2 GluR-B GluR-K2 Glutamate receptor ionotropic, AMPA 2 AMPA-selective glutamate receptor 2 A family of AMPA-selective glutamate receptors. Keinaenen K. Wisden W. Sommer B. Werner P. Herb A. Verdoorn T.A. Sakmann B. Seeburg P.H. 1990 Science 249 556-560 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS FLIP AND FLOP) Brain Molecular cloning and functional expression of glutamate receptor subunit genes. Boulter J. Hollmann M. O'Shea-Greenfield A. Hartley M. Deneris E.S. Maron C. Heinemann S.F. 1990 Science 249 1033-1037 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM FLOP) A family of glutamate receptor genes: evidence for the formation of heteromultimeric receptors with distinct channel properties. Nakanishi N. Schneider N.A. Axel R. doi:10.1016/0896-6273(90)90212-X 1990 Neuron 5 569-581 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM FLIP) Brain cortex Hippocampus N-glycosylation is not a prerequisite for glutamate receptor function but is essential for lectin modulation. Everts I. Villmann C. Hollmann M. 1997 Mol. Pharmacol. 52 861-873 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM FLIP) FUNCTION Sprague-Dawley The AMPA receptor GluR2 C terminus can mediate a reversible, ATP-dependent interaction with NSF and alpha- and beta-SNAPs. Osten P. Srivastava S. Inman G.J. Vilim F.S. Khatri L. Lee L.M. States B.A. Einheber S. Milner T.A. Hanson P.I. Ziff E.B. doi:10.1016/S0896-6273(00)80518-8 1998 Neuron 21 99-110 SUBCELLULAR LOCATION TISSUE SPECIFICITY INTERACTION WITH NSF IDENTIFICATION IN A COMPLEX WITH NSF; NAPA AND NAPB MUTAGENESIS OF 851-ASN-PRO-852 Clustering of AMPA receptors by the synaptic PDZ domain-containing protein PICK1. Xia J. Zhang X. Staudinger J. Huganir R.L. doi:10.1016/S0896-6273(00)80689-3 1999 Neuron 22 179-187 INTERACTION WITH PRKCABP Flip and flop: a cell-specific functional switch in glutamate-operated channels of the CNS. Sommer B. Keinaenen K. Verdoorn T.A. Wisden W. Burnashev N. Herb A. Koehler M. Takagi T. Sakmann B. Seeburg P.H. 1990 Science 249 1580-1585 ALTERNATIVE SPLICING (ISOFORMS FLIP AND FLOP) Antibody specific for phosphorylated AMPA-type glutamate receptors at GluR2 Ser-696. Nakazawa K. Tadakuma T. Nokihara K. Ito M. doi:10.1016/0168-0102(95)00977-9 1995 Neurosci. Res. 24 75-86 PHOSPHORYLATION AT SER-683 AND SER-717 GRIP: a synaptic PDZ domain-containing protein that interacts with AMPA receptors. Dong H. O'Brien R.J. Fung E.T. Lanahan A.A. Worley P.F. Huganir R.L. doi:10.1038/386279a0 1997 Nature 386 279-284 INTERACTION WITH GRIP1 Hippocampus Association of AMPA receptors with a subset of glutamate receptor-interacting protein in vivo. Wyszynski M. Valtschanoff J.G. Naisbitt S. Dunah A.W. Kim E. Standaert D.G. Weinberg R. Sheng M. 1999 J. Neurosci. 19 6528-6537 INTERACTION WITH GRIP2 Glutamatergic plasticity by synaptic delivery of GluR-B(long)-containing AMPA receptors. Kolleker A. Zhu J.J. Schupp B.J. Qin Y. Mack V. Borchardt T. Koehr G. Malinow R. Seeburg P.H. Osten P. doi:10.1016/S0896-6273(03)00722-0 2003 Neuron 40 1199-1212 IDENTIFICATION OF ISOFORM 3 SUBCELLULAR LOCATION DEVELOPMENTAL STAGE TISSUE SPECIFICITY Tyrosine phosphorylation and regulation of the AMPA receptor by SRC family tyrosine kinases. Hayashi T. Huganir R.L. doi:10.1523/JNEUROSCI.0799-04.2004 2004 J. Neurosci. 24 6152-6160 PHOSPHORYLATION AT TYR-876 TISSUE SPECIFICITY Different domains of the AMPA receptor direct stargazin-mediated trafficking and stargazin-mediated modulation of kinetics. Bedoukian M.A. Weeks A.M. Partin K.M. doi:10.1074/jbc.M600679200 2006 J. Biol. Chem. 281 23908-23921 SUBCELLULAR LOCATION INTERACTION WITH CACNG2 Structure of a glutamate-receptor ligand-binding core in complex with kainate. Armstrong N. Sun Y. Chen G.Q. Gouaux E. doi:10.1038/27692 1998 Nature 395 913-917 X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 404-796 IN COMPLEX WITH KAINATE Mechanisms for activation and antagonism of an AMPA-sensitive glutamate receptor: crystal structures of the GluR2 ligand binding core. Armstrong N. Gouaux E. doi:10.1016/S0896-6273(00)00094-5 2000 Neuron 28 165-181 X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 413-796 IN COMPLEXES WITH GLUTAMATE; AMPA; KAINATE; DNQX AND ZINC Mechanism of activation and selectivity in a ligand-gated ion channel: structural and functional studies of GluR2 and quisqualate. Jin R. Horning M. Mayer M.L. Gouaux E. doi:10.1021/bi020583k 2002 Biochemistry 41 15635-15643 X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 413-796 IN COMPLEX WITH QUISQUALATE FUNCTION Structural basis for AMPA receptor activation and ligand selectivity: crystal structures of five agonist complexes with the GluR2 ligand-binding core. Hogner A. Kastrup J.S. Jin R. Liljefors T. Mayer M.L. Egebjerg J. Larsen I.K. Gouaux E. doi:10.1016/S0022-2836(02)00650-2 2002 J. Mol. Biol. 322 93-109 X-RAY CRYSTALLOGRAPHY (1.46 ANGSTROMS) OF 413-796 IN COMPLEXES WITH ACPA AND BR-HIBO Mechanism of glutamate receptor desensitization. Sun Y. Olson R. Horning M. Armstrong N. Mayer M. Gouaux E. doi:10.1038/417245a 2002 Nature 417 245-253 X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 413-796 IN COMPLEXES WITH AMPA; DNQX AND KAINATE FUNCTION SUBUNIT MUTAGENESIS OF LEU-504 AND ASN-775 Three-dimensional structure of the ligand-binding core of GluR2 in complex with the agonist (S)-ATPA: implications for receptor subunit selectivity. Lunn M.-L. Hogner A. Stensboel T.B. Gouaux E. Egebjerg J. Kastrup J.S. doi:10.1021/jm021020+ 2003 J. Med. Chem. 46 872-875 X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 413-796 IN COMPLEXES WITH ATPA AND ZINC IONS Structural basis for partial agonist action at ionotropic glutamate receptors. Jin R. Banke T.G. Mayer M.L. Traynelis S.F. Gouaux E. doi:10.1038/nn1091 2003 Nat. Neurosci. 6 803-810 X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 413-796 IN COMPLEXES WITH WILLARDIINES FUNCTION Tuning activation of the AMPA-sensitive GluR2 ion channel by genetic adjustment of agonist-induced conformational changes. Armstrong N. Mayer M. Gouaux E. doi:10.1073/pnas.1037393100 2003 Proc. Natl. Acad. Sci. U.S.A. 100 5736-5741 X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 413-796 IN COMPLEXES WITH AMPA; KAINATE AND QUISQUALATE FUNCTION Mechanism of positive allosteric modulators acting on AMPA receptors. Jin R. Clark S. Weeks A.M. Dudman J.T. Gouaux E. Partin K.M. doi:10.1523/JNEUROSCI.2567-05.2005 2005 J. Neurosci. 25 9027-9036 X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 413-796 IN COMPLEXES WITH ANIRACETAM AND CX614 FUNCTION Tyr702 is an important determinant of agonist binding and domain closure of the ligand-binding core of GluR2. Frandsen A. Pickering D.S. Vestergaard B. Kasper C. Nielsen B.B. Greenwood J.R. Campiani G. Fattorusso C. Gajhede M. Schousboe A. Kastrup J.S. doi:10.1124/mol.104.002931 2005 Mol. Pharmacol. 67 703-713 X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 413-796 IN COMPLEXES WITH CPW399 AND KAINATE FUNCTION Measurement of conformational changes accompanying desensitization in an ionotropic glutamate receptor. Armstrong N. Jasti J. Beich-Frandsen M. Gouaux E. doi:10.1016/j.cell.2006.08.037 2006 Cell 127 85-97 X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 413-794 FUNCTION MASS SPECTROMETRY The structure of a mixed GluR2 ligand-binding core dimer in complex with (S)-glutamate and the antagonist (S)-NS1209. Kasper C. Pickering D.S. Mirza O. Olsen L. Kristensen A.S. Greenwood J.R. Liljefors T. Schousboe A. Waetjen F. Gajhede M. Sigurskjold B.W. Kastrup J.S. doi:10.1016/j.jmb.2006.01.024 2006 J. Mol. Biol. 357 1184-1201 X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 413-796 IN COMPLEX WITH GLUTAMATE AND S1209 FUNCTION Gria2 Glur2 Ionotropic glutamate receptor. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. Binding of the excitatory neurotransmitter L-glutamate induces a conformation change, leading to the opening of the cation channel, and thereby converts the chemical signal to an electrical impulse. The receptor then desensitizes rapidly and enters a transient inactive state, characterized by the presence of bound agonist. Homotetramer or heterotetramer of pore-forming glutamate receptor subunits. Tetramers may be formed by the dimerization of dimers. May interact with MPP4. Forms a ternary complex with GRIP1 and CSPG4 (By similarity). Interacts with CACNG2, PRKCABP, GRIP1 and GRIP2. Interacts with NSF via its C-terminus. Part of a complex containing GRIA2, NSF and NAPA and/or NAPB. Interaction with CACNG2 promotes cell surface expression. Detected in forebrain. Detected in dendrites of neuronal cells. Detected at low levels in newborns. Levels increase strongly and are highest in hippocampus from 8 to 14 day old animals. Detected at intermediate levels at day 42 (at protein level). Palmitoylated. Depalmitoylated upon glutamate stimulation. Cys-610 palmitoylation leads to Golgi retention and decreased cell surface expression. In contrast, Cys-836 palmitoylation does not affect cell surface expression but regulates stimulation-dependent endocytosis (By similarity). Fully edited in the brain. Heteromerically expressed edited GLUR2 (R) receptor complexes are impermeable to calcium, whereas the unedited (Q) forms are highly permeable to divalent ions (By similarity). 607 The postsynaptic actions of Glu are mediated by a variety of receptors that are named according to their selective agonists. This receptor binds AMPA (quisqualate) > glutamate > kainate. Belongs to the glutamate-gated ion channel (TC 1.A.10) family. 1 21 Glutamate receptor 2 22 883 Extracellular 22 543 544 564 Cytoplasmic 565 624 625 645 Extracellular 646 812 813 833 Cytoplasmic 834 883 Glutamate binding 499 501 Glutamate binding 675 676 Glutamate 506 506 Glutamate 726 726 Phosphoserine; by PKC 683 683 Phosphoserine; by PKG 717 717 Phosphotyrosine 869 869 Phosphotyrosine 876 876 Phosphoserine 880 880 S-palmitoyl cysteine 610 610 S-palmitoyl cysteine 836 836 N-linked (GlcNAc...) 256 256 N-linked (GlcNAc...) 370 370 N-linked (GlcNAc...) 406 406 N-linked (GlcNAc...) 413 413 In isoform Flip. TP 765 766 In isoform Flip. S 775 775 In isoform Flip. V 779 779 In isoform Flip. AKDSG 796 800 In isoform 3. MTLSDVMRSKARLSITGSTGENGRVMTPEFPKAVHAVPYVSPGMGMNVSVTDLS 848 883 In RNA edited version. R 607 607 Promotes dimerization. Strongly reduced desensitization Y 504 504 Increases rate of desensitization D 775 775 Strongly reduces interaction with NSF AA 851 852 416 420 424 426 427 429 433 435 438 441 442 444 445 457 461 465 476 478 483 489 494 496 504 507 510 512 516 519 521 526 657 662 664 671 675 682 686 697 704 706 707 716 717 719 720 726 727 733 741 745 751 753 756 758 764 776 779 788 789 791 false 4 Grip2 false 1 Mpp4 true 1 NSF false 4 Nsf false 6 Pick1 EMBL EMBL EMBL EMBL EMBL PIR RefSeq RefSeq UniGene PDB 1.90 A/B/C=413-796 PDB 1.60 A=404-796 PDB 1.80 A/B=413-796 PDB 1.70 A/B/C=413-796 PDB 2.00 A/B=413-796 PDB 1.90 A=413-796 PDB 1.90 A=404-796 PDB 2.30 A/B=413-796 PDB 2.30 A/B=413-796 PDB 2.10 A=413-796 PDB 1.80 A/B/C=413-796 PDB 1.85 A/B/C=413-796 PDB 1.65 A=413-796 PDB 1.73 A=413-796 PDB 1.46 A/B/C=413-796 PDB 1.95 A/B/C=413-796 PDB 2.15 A/B=413-796 PDB 1.65 A/B/C=413-796 PDB 1.46 A/B/C/D=413-794 PDB 2.15 A/B=413-796 PDB 1.80 A=413-796 PDB 1.35 A=413-796 PDB 1.65 A=413-796 PDB 1.97 A/B/C=413-796 PDB 1.80 A/B/C=413-796 PDB 1.95 A/B/C=413-796 PDB 1.90 A/B/C=413-796 PDB 2.00 A/B/C=413-796 PDB 1.95 A/B/C=413-796 PDB 1.90 A/B/C=413-796 PDB 1.90 A/B/C=413-796 PDB 1.90 A/B/C=413-796 PDB 1.80 A/B/C=413-796 PDB 1.75 A/B/C=413-796 PDB 1.90 A/B/C=413-796 PDB 2.10 A/B/C=413-796 PDB 1.85 A=413-796 PDB 1.90 A/B=413-796 PDB 1.60 A=413-796 PDB 1.60 A=413-796 PDB 2.00 A/B/C=413-796 PDB 2.00 A/B=413-796 PDB 1.80 A/B=413-796 PDB 1.80 A=413-796 PDB 2.10 A/B=413-796 PDB 1.75 A=652-796 PDB 1.85 A=413-796 PDB 2.17 A=413-796 PDB 1.70 A/B/C/D/E/F=413-796 PDB 1.65 A/B=413-796 PDB 2.10 A=413-796 PDB 2.65 A/B=413-796 PDB 1.54 A/B/C=652-795 PDB 2.40 A/B/C/D=413-794 PDB 2.30 A/B=413-794 PDB 2.26 A/B=413-527 A/B=652-796 PDB 2.38 A/B/C=412-527 PDB 2.25 A/B=413-527 A/B=652-796 PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum IntAct PhosphoSite Ensembl Rattus norvegicus GeneID KEGG RGD Gria2 HOVERGEN DrugBank Cyclothiazide LinkHub ArrayExpress GermOnline Rattus norvegicus InterPro ANF_lig_bd_rcpt InterPro Glutamate_receptor-rel InterPro Iontro_glu_rcpt InterPro NMDA_rcpt PANTHER Glut_Rec_Related 1 Pfam ANF_receptor 1 Pfam Lig_chan 1 PRINTS NMDARECEPTOR SMART PBPe 1 UniProtKB UniProtKB UniProtKB UniProtKB UniProtKB UniProtKB UniProtKB UniProtKB UniProtKB UniProtKB UniProtKB UniProtKB UniProtKB 1998-07-15 2 true 98688 Flop MQKIMHISVL LSPVLWGLIF GVSSNSIQIG GLFPRGADQE YSAFRVGMVQ FSTSEFRLTP HIDNLEVANS FAVTNAFCSQ FSRGVYAIFG FYDKKSVNTI TSFCGTLHVS FITPSFPTDG THPFVIQMRP DLKGALLSLI EYYQWDKFAY LYDSDRGLST LQAVLDSAAE KKWQVTAINV GNINNDKKDE TYRSLFQDLE LKKERRVILD CERDKVNDIV DQVITIGKHV KGYHYIIANL GFTDGDLLKI QFGGANVSGF QIVDYDDSLV SKFIERWSTL EEKEYPGAHT ATIKYTSALT YDAVQVMTEA FRNLRKQRIE ISRRGNAGDC LANPAVPWGQ GVEIERALKQ VQVEGLSGNI KFDQNGKRIN YTINIMELKT NGPRKIGYWS EVDKMVVTLT ELPSGNDTSG LENKTVVVTT ILESPYVMMK KNHEMLEGNE RYEGYCVDLA AEIAKHCGFK YKLTIVGDGK YGARDADTKI WNGMVGELVY GKADIAIAPL TITLVREEVI DFSKPFMSLG ISIMIKKPQK SKPGVFSFLD PLAYEIWMCI VFAYIGVSVV LFLVSRFSPY EWHTEEFEDG RETQSSESTN EFGIFNSLWF SLGAFMQQGC DISPRSLSGR IVGGVWWFFT LIIISSYTAN LAAFLTVERM VSPIESAEDL SKQTEIAYGT LDSGSTKEFF RRSKIAVFDK MWTYMRSAEP SVFVRTTAEG VARVRKSKGK YAYLLESTMN EYIEQRKPCD TMKVGGNLDS KGYGIATPKG SSLGNAVNLA VLKLNEQGLL DKLKNKWWYD KGECGSGGGD SKEKTSALSL SNVAGVFYIL VGGLGLAMLV ALIEFCYKSR AEAKRMKVAK NPQNINPSSS QNSQNFATYK EGYNVYGIES VKI Flip 3 Long