Ionotropic glutamate receptors in the retina: Moving from molecules to circuits

Ionotropic glutamate receptors in the retina: Moving from molecules to circuits The cloning of the glutamate-gated ion channels of the brain revealed an unexpected level of complexity: there are many different genes that encode distinct subunits of the receptor/channel complex and an even larger number of possible receptor subunit combinations. Many—nearly all—of these gene products are expressed in the retina, and the questions that we face today are: how are they used and why are there so many? Answers to these questions will be found at several levels. At the level of transcription, we have learned that different sets of subunits are expressed by different retinal neurons. Little is known about the transcriptional control of these genes, so it remains to be determined whether these patterns of expression reflect the need for different gene products in different retinal neurons or whether these patterns of expression reflect the functional constraints of gene expression. Another level of complexity is caused by alternative splicing, and here we report that at least four and possibly all eight of the different NMDAR1 transcripts are present in the mouse retina. The consequences of this alternative splicing are poorly understood, but antibodies directed against the two different possible C-termini of NMDAR1 label many of the same cell types. It is possible that these different splice variants are combined to generate the channels. While immunohistochemistry provides us with a glimpse of the subunit proteins, much remains to be learned about their half-life within a retinal cell, their intracellular trafficking, their regulation at the synapse, and the proteins associated with their cytoplasmic domains. An approach we have taken towards studying the dynamic properties of receptor subunits has been to fuse them to the cDNA encoding the jellyfish Green Fluorescent Protein. This makes it possible to follow functional subunits in transfected cells over time and to begin to measure the mobility of the protein. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Vision Research Elsevier

Ionotropic glutamate receptors in the retina: Moving from molecules to circuits

Vision Research, Volume 38 (10) – May 1, 1998

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Publisher
Elsevier
Copyright
Copyright © 1998 Elsevier Science Ltd
ISSN
0042-6989
eISSN
1878-5646
D.O.I.
10.1016/S0042-6989(98)00008-X
Publisher site
See Article on Publisher Site

Abstract

The cloning of the glutamate-gated ion channels of the brain revealed an unexpected level of complexity: there are many different genes that encode distinct subunits of the receptor/channel complex and an even larger number of possible receptor subunit combinations. Many—nearly all—of these gene products are expressed in the retina, and the questions that we face today are: how are they used and why are there so many? Answers to these questions will be found at several levels. At the level of transcription, we have learned that different sets of subunits are expressed by different retinal neurons. Little is known about the transcriptional control of these genes, so it remains to be determined whether these patterns of expression reflect the need for different gene products in different retinal neurons or whether these patterns of expression reflect the functional constraints of gene expression. Another level of complexity is caused by alternative splicing, and here we report that at least four and possibly all eight of the different NMDAR1 transcripts are present in the mouse retina. The consequences of this alternative splicing are poorly understood, but antibodies directed against the two different possible C-termini of NMDAR1 label many of the same cell types. It is possible that these different splice variants are combined to generate the channels. While immunohistochemistry provides us with a glimpse of the subunit proteins, much remains to be learned about their half-life within a retinal cell, their intracellular trafficking, their regulation at the synapse, and the proteins associated with their cytoplasmic domains. An approach we have taken towards studying the dynamic properties of receptor subunits has been to fuse them to the cDNA encoding the jellyfish Green Fluorescent Protein. This makes it possible to follow functional subunits in transfected cells over time and to begin to measure the mobility of the protein.

Journal

Vision ResearchElsevier

Published: May 1, 1998

References

  • Cloned glutamate receptors
    Hollmann, M.; Heinemann, S.
  • Tetanus toxin binding to isolated and cultured rat retinal glial cells
    Huba, R.; Hofmann, H.-D.
  • Changes in expression of glutamate receptor subunits following photoreceptor degeneration in the rd mouse retina
    Duvoisin, R.M.; Zhang, C.; Hamassaki-Britto, D.E.; Britto, L.R.
  • Expression of NMDA and high-affinity kainate receptor subunit mRNAs in the adult rat retina
    Brandstatter, J.H.; Hartveit, E.; Sassoe-Pognetto, M.; Wässle, H.
  • Membrane currents evoked by ionotropic glutamate receptor agonists in rod bipolar cells in the rat retinal slice preparation
    Hartveit, E.
  • Mobility and detergent extractability of acetylcholine receptors on cultured rat myotubes: a correlation
    Stya, M.; Axelrod, D.
  • Impairment of pupillary responses and optokinetic nystagmus in the Mglur6-deficient mouse
    Iwakabe, H.; Katsuura, G.; Ishibashi, C.; Nakanishi, S.
  • Live astrocytes visualized by green fluorescent protein in transgenic mice
    Zhuo, L.; Sun, B.; Zhang, C.L.; Fine, A.; Chiu, S.Y.; Messing, A.

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