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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, 2019, 2 (1)
doi: 10.1038/s42003-019-0320-y
Artikel, Zweitveröffentlichung, Verlagsversion

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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 KcvATCV-1 to the isolated glutamatebinding 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 KcvATCV-1. 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: Zweitveröffentlichung
Titel: Coupling of a viral K+-channel with a glutamate-binding-domain highlights the modular design of ionotropic glutamate-receptors
Sprache: Englisch
Publikationsjahr: 2019
Publikationsdatum der Erstveröffentlichung: 2019
Verlag: Springer Nature
Titel der Zeitschrift, Zeitung oder Schriftenreihe: Communications Biology
Jahrgang/Volume einer Zeitschrift: 2
(Heft-)Nummer: 1
DOI: 10.1038/s42003-019-0320-y
URL / URN: https://doi.org/10.1038/s42003-019-0320-y
Herkunft: Zweitveröffentlichung aus gefördertem Golden Open Access
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 KcvATCV-1 to the isolated glutamatebinding 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 KcvATCV-1. 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.

Status: Verlagsversion
URN: urn:nbn:de:tuda-tuprints-86030
Sachgruppe der Dewey Dezimalklassifikatin (DDC): 500 Naturwissenschaften und Mathematik > 570 Biowissenschaften, Biologie
Fachbereich(e)/-gebiet(e): 10 Fachbereich Biologie
10 Fachbereich Biologie > Neurophysiologie und neurosensorische Systeme
Hinterlegungsdatum: 07 Apr 2019 19:55
Letzte Änderung: 07 Apr 2019 19:55
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