Light and electron microscopic localization of glutamate immunoreactivity in the supraoptic nucleus of the rat hypothalamus

Meeker, Rick B.; Swanson, D.J.; Hayward, James N.

doi:10.1016/0306-4522(89)90318-7

Cited by 72 publications

(53 citation statements)

References 17 publications

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“…Biogenesis and assembly of nAChR are enhanced by the binding of nicotine (43,44). Similarly, binding of glutamate, which exists in the endoplasmic reticulum at high concentrations (45), could influence AMPAR assembly as well, albeit negatively. Although no open state structure is yet available for iGluRs, significant displacements of TM helices could be induced by ligand binding at the LBD during iGluR gating (46 -48), similar to K ϩ channels (49).…”

Section: Discussionmentioning

confidence: 99%

The Transmembrane Domain Mediates Tetramerization of α-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid (AMPA) Receptors

Gan¹,

Dai

Zhou

et al. 2016

Journal of Biological Chemistry

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AMPA receptors (AMPARs) mediate fast excitatory neurotransmission in the central nervous system. Functional AMPARs are tetrameric complexes with a highly modular structure, consisting of four evolutionarily distinct structural domains: an amino-terminal domain (ATD), a ligand-binding domain (LBD), a channel-forming transmembrane domain (TMD), and a carboxyl-terminal domain (CTD). Here we show that the isolated TMD of the GluA1 AMPAR is fully capable of tetramerization. Additionally, removal of the extracellular domains from the receptor did not affect membrane topology or surface delivery. Furthermore, whereas the ATD and CTD contribute positively to tetramerization, the LBD presents a barrier to the process by reducing the stability of the receptor complex. These experiments pinpoint the TMD as the "tetramerization domain" for AMPARs, with other domains playing modulatory roles. They also raise intriguing questions about the evolution of iGluRs as well as the mechanisms regulating the biogenesis of AMPAR complexes.

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Section: Discussionmentioning

confidence: 99%

The Transmembrane Domain Mediates Tetramerization of α-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid (AMPA) Receptors

Gan¹,

Dai

Zhou

et al. 2016

Journal of Biological Chemistry

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“…Unfortunately, the actual glutamate levels are not known, but glutamate is present in the ER and other compartments of the secretory pathway in amounts detectable by immunochemical staining (Meeker et al, 1989). Based on studies with synthetic model compounds, the ER membrane, unlike most other cellular membranes, is permeable to small molecules (Le Gall et al, 2004).…”

Section: Discussionmentioning

confidence: 99%

Agonist Occupancy Is Essential for Forward Trafficking of AMPA Receptors

Coleman¹,

Möykkynen²,

Jouppila³

et al. 2009

J. Neurosci.

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“…So how might GluR function be related to trafficking? Glutamate, the natural agonist, is prevalent intracellularly at 4 -14 mM concentrations (Berger et al, 1977;Shank and Aprison, 1988), much of this associated with the ER (Meeker et al, 1989). Given the affinity for glutamate binding to GluRs is in the 50 -250 nM range, it follows that nascent GluR subunits would rapidly isomerize to their glutamate-bound conformation, perhaps before assembly, and that oligomeric GluRs also would naturally exist in a bound conformation.…”

Section: Functional Quality Controlmentioning

confidence: 99%

Glutamate Receptor Trafficking: Endoplasmic Reticulum Quality Control Involves Ligand Binding and Receptor Function

Mah

Cornell²,

Mitchell³

et al. 2005

J. Neurosci.

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The glutamate receptor (GluR) agonist-binding site consists of amino acid residues in the extracellular S1 and S2 domains in the N-terminal and M3-M4 loop regions, respectively. In the present study, we sought to confirm that the conserved ligand-binding residues identified in the AMPA receptor S1S2 domains also participate in ligand binding of GluR6 kainate receptors. Amino acid substitutions were made in the GluR6 parent at R523, T690, and E738 to alter their potential interactions with ligand. Mutant receptors were expressed in human embryonic kidney 293 cells, confirmed by Western blot analysis, and tested by [

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Light and electron microscopic localization of glutamate immunoreactivity in the supraoptic nucleus of the rat hypothalamus

Cited by 72 publications

References 17 publications

The Transmembrane Domain Mediates Tetramerization of α-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid (AMPA) Receptors

The Transmembrane Domain Mediates Tetramerization of α-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid (AMPA) Receptors

Agonist Occupancy Is Essential for Forward Trafficking of AMPA Receptors

Glutamate Receptor Trafficking: Endoplasmic Reticulum Quality Control Involves Ligand Binding and Receptor Function

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