Betz, H. ; Kuhse, J. ; Schmieden, V. ; Laube, Bodo ; Kirsch, J. ; Harvey, R. J. (1999)
Structure and functions of inhibitory and excitatory glycine receptors.
In: Annals of the New York Academy of Sciences, 868
Artikel, Bibliographie
Kurzbeschreibung (Abstract)
The strychnine-sensitive glycine receptor (GlyR) is a pentameric chloride channel protein that exists in several developmentally and regionally regulated isoforms in the CNS. These result from the differential expression of four genes encoding different variants (alpha 1-alpha 4) of the ligand-binding subunit of the GlyR. Their assembly with the structural beta subunit is governed by "assembly cassettes" within the extracellular domains of these proteins and creates chloride channels of distinct conductance properties. GlyR gating is potentiated by Zn2+, a metal ion co-released with different neurotransmitters. Site-directed mutagenesis has unraveled major determinants of agonist binding and Zn2+ potentiation. During development, glycine receptors mediate excitation that results in Ca2+ influx and neurotransmitter release. Ca2+ influx triggered by the activation of embryonic GlyRs is required for the synaptic localization of the GlyR and its anchoring protein gepyhrin. In the adult, mutations in GlyR-subunit genes result in motor disorders. The spastic and spasmodic phenotypes in mouse as well as human hereditary startle disease will be discussed.
| Typ des Eintrags: | Artikel |
|---|---|
| Erschienen: | 1999 |
| Autor(en): | Betz, H. ; Kuhse, J. ; Schmieden, V. ; Laube, Bodo ; Kirsch, J. ; Harvey, R. J. |
| Art des Eintrags: | Bibliographie |
| Titel: | Structure and functions of inhibitory and excitatory glycine receptors. |
| Sprache: | Englisch |
| Publikationsjahr: | 1999 |
| Titel der Zeitschrift, Zeitung oder Schriftenreihe: | Annals of the New York Academy of Sciences |
| Jahrgang/Volume einer Zeitschrift: | 868 |
| Kurzbeschreibung (Abstract): | The strychnine-sensitive glycine receptor (GlyR) is a pentameric chloride channel protein that exists in several developmentally and regionally regulated isoforms in the CNS. These result from the differential expression of four genes encoding different variants (alpha 1-alpha 4) of the ligand-binding subunit of the GlyR. Their assembly with the structural beta subunit is governed by "assembly cassettes" within the extracellular domains of these proteins and creates chloride channels of distinct conductance properties. GlyR gating is potentiated by Zn2+, a metal ion co-released with different neurotransmitters. Site-directed mutagenesis has unraveled major determinants of agonist binding and Zn2+ potentiation. During development, glycine receptors mediate excitation that results in Ca2+ influx and neurotransmitter release. Ca2+ influx triggered by the activation of embryonic GlyRs is required for the synaptic localization of the GlyR and its anchoring protein gepyhrin. In the adult, mutations in GlyR-subunit genes result in motor disorders. The spastic and spasmodic phenotypes in mouse as well as human hereditary startle disease will be discussed. |
| Fachbereich(e)/-gebiet(e): | 10 Fachbereich Biologie 10 Fachbereich Biologie > Neurophysiologie und neurosensorische Systeme ?? fb10_zoologie ?? |
| Hinterlegungsdatum: | 11 Apr 2011 13:37 |
| Letzte Änderung: | 05 Mär 2019 06:48 |
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