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Structure, diversity and synaptic localization of inhibitory glycine receptors.

Betz, H. ; Kuhse, J. ; Fischer, M. ; Schmieden, V. ; Laube, Bodo ; Kuryatov, A. ; Langosch, D. ; Meyer, G. ; Bormann, J. ; Rundström, N. :
Structure, diversity and synaptic localization of inhibitory glycine receptors.
In: Journal of physiology, Paris, 88 (4) pp. 243-8. ISSN 0928-4257
[Artikel], (1994)

Kurzbeschreibung (Abstract)

The inhibitory glycine receptor (GlyR) mediates postsynaptic inhibition in spinal cord, brain stem and other regions of the vertebrate central nervous system. Biochemical and molecular approaches have identified different developmentally and regionally regulated GlyR isoforms that result from the differential expression of at least four genes coding for different variants of the ligand-binding alpha subunit. Molecular studies have allowed identification of GlyR subunit domains implicated in ligand binding, channel formation and receptor assembly. At the postsynaptic membrane, the GlyR colocalizes with a 93-kDa tubulin-binding peripheral membrane protein, gephyrin. Antisense inhibition of gephyrin expression prevents GlyR accumulation at postsynaptic membrane specialization. Thus, gephyrin is essential for postsynaptic receptor topology.

Typ des Eintrags: Artikel
Erschienen: 1994
Autor(en): Betz, H. ; Kuhse, J. ; Fischer, M. ; Schmieden, V. ; Laube, Bodo ; Kuryatov, A. ; Langosch, D. ; Meyer, G. ; Bormann, J. ; Rundström, N.
Titel: Structure, diversity and synaptic localization of inhibitory glycine receptors.
Sprache: Englisch
Kurzbeschreibung (Abstract):

The inhibitory glycine receptor (GlyR) mediates postsynaptic inhibition in spinal cord, brain stem and other regions of the vertebrate central nervous system. Biochemical and molecular approaches have identified different developmentally and regionally regulated GlyR isoforms that result from the differential expression of at least four genes coding for different variants of the ligand-binding alpha subunit. Molecular studies have allowed identification of GlyR subunit domains implicated in ligand binding, channel formation and receptor assembly. At the postsynaptic membrane, the GlyR colocalizes with a 93-kDa tubulin-binding peripheral membrane protein, gephyrin. Antisense inhibition of gephyrin expression prevents GlyR accumulation at postsynaptic membrane specialization. Thus, gephyrin is essential for postsynaptic receptor topology.

Titel der Zeitschrift, Zeitung oder Schriftenreihe: Journal of physiology, Paris
Band: 88
(Heft-)Nummer: 4
Fachbereich(e)/-gebiet(e): Fachbereich Biologie, Biology > Zelluläre Neurophysiologie, Neurosensory Systems
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Fachbereich Biologie, Biology
Hinterlegungsdatum: 12 Apr 2011 11:24
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