4 edition of A topology model for glutamate receptor subunit, GluR6 found in the catalog.
A topology model for glutamate receptor subunit, GluR6
Melissa Mien Tan
Thesis (M.Sc.) -- University of Toronto, 1998.
|Series||Canadian theses = -- Thèses canadiennes|
|The Physical Object|
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Abstract Cbimeric receptor subunits of the AMPA receptor subunit GluR2 and the kainate receptor subunit GluR6 were constructed and stably expressed in baby hamster kidney cells. By using Ca*+ imaging and radioligand binding, we demonstrated that substitution of a . Glutamate receptor subunits were originally proposed to have the same transmembrane topology as the subunits for other ligand-gated ion channels, such as the nicotinic acetylcholine receptor and the GABA A receptor, with a large N-terminal extracellular domain, four transmembrane domains (TM1-TM4), and an extracellular C-terminus.
Roche KW, Raymond LA, Blackstone C, Huganir RL. Transmembrane topology of the glutamate receptor subunit GluR6. J Biol Chem. Apr 22; (16)– Taverna FA, Wang LY, MacDonald JF, Hampson DR. A transmembrane model for an ionotropic glutamate receptor predicted on the basis of the location of asparagine-linked oligosaccharides. We report the crystal structure of the glycosylated ligand-binding (S1S2) domain of the kainate receptor subunit GluR6, in complex with the agonist domoate. The structure shows the expected overall homology with AMPA and NMDA receptor subunit structures but reveals an unexpected binding mode for the side chain of domoate, in which contact is made to the larger lobe only (lobe I).
Glutamate Receptor Glycogen Metabolism Membrane Topology Glutamate Receptor Subunit Regulatory Phosphorylation Site These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves. The past fifteen years has seen a revolution in our understanding of ionotropic glutamate receptor (iGluR) structure, starting with the first view of the ligand binding domain (LBD) published in , and in many ways culminating in the publication of the full-length structure of GluA2 in
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A topology model for glutamate receptor subunit, GluR6 Melissa Mien Tan, Institute of Medic& Science University of Toron to ABSTRACT The topology of GluR6, a glutarnate receptor subunit, was determined using mutagenesis, expression Author: Melissa Mien Tan. Abstract. It has been only 6 years since the expression cloning of the first glutamate receptor (GluR) cDNA (Hollmann et al, ), but in this short period of time, a true explosion took place of our knowledge of the molecular makeup of the central nervous system’s most abundant and most important excitatory amino acid receptor by: 5.
Topology Profile for a Glutamate Receptor: sults support a topological model for glutamate recep- tor subunits that consists of three transmembrane do- mains, M1, M3, and M4, and another domain, the a native glycosylation site in the kainate receptor subunit GluR6.
Our results with the AMPA receptor subunit. Abstract. Glutamate receptors are large integral membrane proteins that belong to the class of ligand-gated ion channels.
They constitute a family of receptors that are activated by binding of the neurotransmitter onal receptors are formed by assembly of several subunits around a central ion-conducting by: 1. Dansmembrane Topology of Glutamate Receptor Subunit GluR6 acids based on mature protein (13)) mutation.
The fidelity of the mu- tation was confirmed by DNA sequencing. Dansient Expression of GluR6 in HEK Cells-The cDNA encod- ing the GluR6 subunit was transiently transfected into human embry. All other chemicals were purchased from Aldrich and Sigma.
Construction of Chimeric Proteins The glutamate receptor subunit pSK-GluR3 (obtained from J. Boulter) Glutamate Receptor Topology was digested with EcoRI and Smal. The supF gene in pcDNAI (In- vitrogen) was replaced by an ampicillan resistance gene, which re- sulted in pcDNA-Amp.
Roche KW, Raymond LA, Blackstone C, Huganir RL. Transmembrane topology of the glutamate receptor subunit GluR6. J Biol Chem. Apr 22; (16)– [Google Scholar] Root MJ, MacKinnon R. Identification of an external divalent cation-binding site in the pore of a cGMP-activated channel.
Neuron. Sep; 11 (3)– At least two different models for the transmembrane topology of the glutamate receptor subunits have been proposed. We investigated some features of these two models for the GluR1 subunit by inserting epitope tags between residues Lys ProAla GluLys Proor after the C-terminal residue Leu The accessibility of the tags then was detected using a tag-specific.
EXPERIMENTAL PROCEDURES. Mutagenesis—The rat kainate receptor subunit GluR6(Q) and a non-desensitizing mutant of the rat AMPA receptor GluR1 (GluR1(LF) ()), as well as C.
elegans subunits GLR1 to GLR8 and NMR1 to NMR2 (), were used for construction of glutamate receptor subunit enable transplantation of domains, identical restriction sites were introduced at. We report the isolation and functional characterization of cDNAs encoding a Drosophila kainate-selective glutamate receptor.
The deduced mature residue protein (DGluR-I) isDa and. For ionotropic glutamate receptors, the agonist-binding sites and associated ion channels are incorporated into the same macromolecular complex.
Agonists increase the probability that the channel will open, and the three classes of ionotropic receptor originally were named after reasonably selective agonists: N-methyl-d-aspartate (NMDA), α-aminohydroxymethylisoxazole propionic acid. The glutamate receptor subunits were first thought to cross the cell membrane four times in a manner analogous to the neuronal nicotinic acetylcholine, GABAA, and glycine receptors.
This model led the field for nearly five years, although it was frequently in conflict with the data. Recently, comparisons with bacterial proteins, epitope tagging experiments, and the construction of chimeras has.
Research Highlights Autism and related models are associated with glutamate receptor dysfunction. Kainate receptor subunit GluR6, and is implicated in ASD. Disruption of synaptic ASD candidate genes disrupts glutamate receptor activity. Glutamate receptors appear to be strong drug targets for specific ASD symptoms.
GluR6 is the major kainate receptor-forming subunit in the striatum, and functional kainate receptors are abolished in medium spiny neurons of GluR6 −/− mice, thus preventing any compensatory changes in terms of kainate receptors Casassus and Mulle,Chergui et al., However, other yet unknown glutamate receptor compensatory.
Taken together, these data show that at kainate concentrations of up to a few µM, only kainate receptors are activated by kainate in CA3 neurons and that these receptors contain the GluR6 subunit. Transmembrane topology of the glutamate receptor subunit GluR6.
Roche KW, Raymond LA, Blackstone C, Huganir RL J Biol Chem, (16), 01 Apr (S1S2) domain of the kainate receptor subunit GluR6, in complex with the agonist domoate. The structure shows the expected overall homology with AMPA and NMDA receptor subunit struc-tures but reveals an unexpected binding mode for the side chain of domoate, in which contact is made to the larger lobe only (lobe I).
a Three Transmembrane Domain Topology for the Glutamate Receptor GluR1 Michael Hollmann,* Cornelia Maron, and Stephen Heinemann tion site in the kainate receptor subunit, GluR6, sug- mer et aL, ). Model 1 is from Hollmann et al. (), model 2 from Kein~nen et al.
(), model 3 from Dingledine et al. This includes 5 subunits of the glutamate receptor ionotropic AMPA glutamate receptor subunits (Glur2, Glur3, Glur4) and kainate receptor subunits (Glur5, Glur6). Glutamate gated ion channels are made up of four subunits per channel with each subunit contributing to the pore loop structure.
We have characterized the phosphorylation of the glutamate receptor subunit GluR1, using biochemical and electrophysiological techniques. GluR1 is phosphorylated on multiple sites that are all located on the C-terminus of the protein. Cyclic AMP-dependent protein kinase specifically phosphorylates SER of GluR1 in transfected HEK cells and in neurons in culture.
Roche KW, Raymond LA, Blackstone C, Huganir RL. Transmembrane topology of the glutamate receptor subunit GluR6. J Biol Chem. Apr 22; (16)– Bennett JA, Dingledine R.
Topology profile for a glutamate receptor: three transmembrane domains and a channel-lining reentrant membrane loop. Neuron. Feb; 14 (2)–Transmembrane topology of the glutamate receptor subunit GluR6. J Biol Chem. Apr 22; (16)– [Google Scholar] Taverna FA, Wang LY, MacDonald JF, Hampson DR.
A transmembrane model for an ionotropic glutamate receptor predicted on the basis of the location of asparagine-linked oligosaccharides.Roche KW, Raymond LA, Blackstone C, Huganir RL () Transmembrane topology of the glutamate receptor subunit glur6.
J Biol Chem – PubMed Google Scholar Ropp JD, Donahue CJ, Wolfgang-Kimball D, Hooley JJ, Chin JYW, Cuthbertson RA, Bauer KD () Aequorea green flourescent protein: simultaneous analysis of wild-type and blue.