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Coupling of a viral K+-channel with a glutamate-binding-domain highlights the modular design of ionotropic glutamate-receptors.

Schönrock, Michael ; Thiel, Gerhard ; Laube, Bodo (2019)
Coupling of a viral K+-channel with a glutamate-binding-domain highlights the modular design of ionotropic glutamate-receptors.
In: Communications biology, 2
doi: 10.1038/s42003-019-0320-y
Artikel, Bibliographie

Kurzbeschreibung (Abstract)

Ionotropic glutamate receptors (iGluRs) mediate excitatory neuronal signaling in the mammalian CNS. These receptors are critically involved in diverse physiological processes; including learning and memory formation, as well as neuronal damage associated with neurological diseases. Based on partial sequence and structural similarities, these complex cation-permeable iGluRs are thought to descend from simple bacterial proteins emerging from a fusion of a substrate binding protein (SBP) and an inverted potassium (K)-channel. Here, we fuse the pore module of the viral K-channel Kcv to the isolated glutamate-binding domain of the mammalian iGluR subunit GluA1 which is structural homolog to SBPs. The resulting chimera (GluATCV*) is functional and displays the ligand recognition characteristics of GluA1 and the K-selectivity of Kcv. These results are consistent with a conserved activation mechanism between a glutamate-binding domain and the pore-module of a K-channel and support the expected phylogenetic link between the two protein families.

Typ des Eintrags: Artikel
Erschienen: 2019
Autor(en): Schönrock, Michael ; Thiel, Gerhard ; Laube, Bodo
Art des Eintrags: Bibliographie
Titel: Coupling of a viral K+-channel with a glutamate-binding-domain highlights the modular design of ionotropic glutamate-receptors.
Sprache: Englisch
Publikationsjahr: 22 Februar 2019
Titel der Zeitschrift, Zeitung oder Schriftenreihe: Communications biology
Jahrgang/Volume einer Zeitschrift: 2
DOI: 10.1038/s42003-019-0320-y
Kurzbeschreibung (Abstract):

Ionotropic glutamate receptors (iGluRs) mediate excitatory neuronal signaling in the mammalian CNS. These receptors are critically involved in diverse physiological processes; including learning and memory formation, as well as neuronal damage associated with neurological diseases. Based on partial sequence and structural similarities, these complex cation-permeable iGluRs are thought to descend from simple bacterial proteins emerging from a fusion of a substrate binding protein (SBP) and an inverted potassium (K)-channel. Here, we fuse the pore module of the viral K-channel Kcv to the isolated glutamate-binding domain of the mammalian iGluR subunit GluA1 which is structural homolog to SBPs. The resulting chimera (GluATCV*) is functional and displays the ligand recognition characteristics of GluA1 and the K-selectivity of Kcv. These results are consistent with a conserved activation mechanism between a glutamate-binding domain and the pore-module of a K-channel and support the expected phylogenetic link between the two protein families.

ID-Nummer: pmid:30820470
Fachbereich(e)/-gebiet(e): 10 Fachbereich Biologie
10 Fachbereich Biologie > Plant Membrane Biophyscis (am 20.12.23 umbenannt in Biologie der Algen und Protozoen)
10 Fachbereich Biologie > Neurophysiologie und neurosensorische Systeme
Hinterlegungsdatum: 05 Mär 2019 06:33
Letzte Änderung: 05 Mär 2019 06:35
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