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AMPA receptor or alpha glutamate receptor

alpha-Amino-3-hydroxy-5-Methylisoxazole-4-Propionic Acid [AMPA] ionophore-linked receptor Function: - the AMPA receptor appears to move in & out of synaptic membranes in a dynamic fashion [5] - endocytosis of AMPA receptors a) may be associated with attenuation of excitatory neurotransmission b) stimulated by synaptic activity, ligand binding & insulin c) dependent on dynamin & phosphorylation/phosphatases d) stimulus for endocytosis determines the fate on the AMPA receptors e) AMPA stimulation leads to a recycling endosome; insulin stimulation leads to degradation? - potentiated by Zn+2. - some variants may be somewhat permeable to Ca+2 - both AMPA & kainate are agonists [4]

Interactions

molecular events

Related

anti-AMPA receptor antibody

General

ionotropic glutamate receptor multisubunit protein Na+ channel quisqualate receptor

Properties

COMPARTMENT: post synaptic membrane CELL-REGION: dendrite CELL: neuron MOTIF: ligand-binding site membrane region ION-PERMEABILITY: Na+ K+ SUBUNITS: AMPA 1 receptor MOTIF: exoplasmic domain {19-536} MOTIF: signal sequence {1-18} N-glycosylation site {N63} N-glycosylation site {N249} N-glycosylation site {N257} N-glycosylation site {N363} N-glycosylation site {N401} N-glycosylation site {N406} Glutamate binding {492-494} binding site SITE: 499-499 FOR-BINDING-OF: Glutamate transmembrane domain {537-557} cytoplasmic loop {558-617} MOTIF: cysteine residue {C603} MODIFICATION: palmitate COMPARTMENT: membrane transmembrane domain {618-638} exoplasmic loop {639-805} MOTIF: Ser phosphorylation site {S645} Glutamate binding {668-669} Ser phosphorylation site {S710} binding site SITE: 719-719 FOR-BINDING-OF: Glutamate transmembrane domain {806-826} cytoplasmic domain {827-906} MOTIF: cysteine residue {C829} MODIFICATION: palmitate COMPARTMENT: membrane Ser phosphorylation site {S849} Ser phosphorylation site {S863} AMPA 2 receptor MOTIF: exoplasmic domain {1-543} MOTIF: signal sequence {1-24} N-glycosylation site {N256} N-glycosylation site {N370} N-glycosylation site {N406} N-glycosylation site {N413} Glutamate binding {499-501} binding site SITE: 506-506 FOR-BINDING-OF: Glutamate transmembrane domain {544-564} cytoplasmic loop {565-624} MOTIF: cysteine residue {C610} MODIFICATION: palmitate COMPARTMENT: membrane transmembrane domain {625-645} exoplasmic loop {646-812} MOTIF: Glutamate binding {675-676} Ser phosphorylation site {S683} Ser phosphorylation site {S717} binding site SITE: 726-726 FOR-BINDING-OF: Glutamate transmembrane domain {813-833} cytoplasmic domain {834-883} MOTIF: cysteine residue {C836} MODIFICATION: palmitate COMPARTMENT: membrane Tyr phosphorylation site {Y869} Tyr phosphorylation site {Y876} Ser phosphorylation site {S880} AMPA 3 receptor MOTIF: exoplasmic domain {1-552} MOTIF: signal sequence {1-28} N-glycosylation site {N63} N-glycosylation site {N266} N-glycosylation site {N380} N-glycosylation site {N415} N-glycosylation site {N422} Glutamate binding {508-510} binding site SITE: 515-515 FOR-BINDING-OF: Glutamate transmembrane domain {553-573} cytoplasmic loop {574-635} MOTIF: cysteine residue {C621} MODIFICATION: palmitate COMPARTMENT: membrane transmembrane domain {636-656} exoplasmic loop {657-823} MOTIF: Glutamate binding {686-687} binding site SITE: 737-737 FOR-BINDING-OF: Glutamate transmembrane domain {824-844} cytoplasmic domain {845-894} MOTIF: cysteine residue {C847} MODIFICATION: palmitate COMPARTMENT: membrane Tyr phosphorylation site {Y877} Tyr phosphorylation site {Y887} AMPA 4 receptor MOTIF: exoplasmic domain {21-544} MOTIF: signal sequence {1-20} N-glycosylation site {N56} N-glycosylation site {N258} N-glycosylation site {N371} N-glycosylation site {N407} N-glycosylation site {N414} Glutamate binding {500-502} binding site SITE: 507-507 FOR-BINDING-OF: Glutamate transmembrane domain {545-565} cytoplasmic loop {566-625} MOTIF: cysteine residue {C611} MODIFICATION: palmitate COMPARTMENT: membrane transmembrane domain {626-646} exoplasmic loop {647-813} MOTIF: Glutamate binding {676-677} binding site SITE: 727-727 FOR-BINDING-OF: Glutamate transmembrane domain {814-834} cytoplasmic domain {835-902} MOTIF: cysteine residue {C837} MODIFICATION: palmitate COMPARTMENT: membrane MISC-INFO: CONDUCTANCE 20 PS INHIBITOR = ALPHA-AMINO-3-HYDROXY-5-METHYLISOXAZOLE-4-PROPIONIC_ACID INHIBITOR = KAINATE

References

  1. Choi 1988
  2. Manzoni OJ, Finiels-Marlier F, Sassetti I, Blockaert J, le Peuch C, Sladeczek FA. The glutamate receptor of the Qp-type activates protein kinase C and is regulated by protein kinase C. Neurosci Lett. 1990 Feb 5;109(1-2):146-51. PMID: 2156190
  3. Barnard EA. Receptor classes and the transmitter-gated ion channels. Trends Biochem Sci. 1992 Oct;17(10):368-74. Review. PMID: 1360717
  4. Lipton SA, Rosenberg PA. Excitatory amino acids as a final common pathway for neurologic disorders. N Engl J Med. 1994 Mar 3;330(9):613-22. Review. No abstract available. PMID: 7905600
  5. Sheng M. Molecular organization of the postsynaptic specialization. Proc Natl Acad Sci U S A. 2001 Jun 19;98(13):7058-61. Review. PMID: 11416187

Component-of

molecular complex

Components

glutamate receptor 1; GluR-1; GluR-A; GluR-K1; glutamate receptor ionotropic, AMPA 1; AMPA-selective glutamate receptor 1 (GRIA1, GLUH1, GLUR1) glutamate receptor 2; GluR-2; GluR-B; GluR-K2; glutamate receptor ionotropic, AMPA 2; AMPA-selective glutamate receptor 2 (GRIA2, GLUR2) glutamate receptor 3; GluR-3; GluR-C; GluR-K3; glutamate receptor ionotropic, AMPA 3; AMPA-selective glutamate receptor 3 (GRIA3, GLUR3, GLURC) glutamate receptor 4; GluR-4; GluR4; GluR-D; glutamate receptor ionotropic, AMPA 4; AMPA-selective glutamate receptor 4 (GRIA4 GLUR4)