TU Darmstadt / ULB / TUbiblio

Fusicoccin Activates KAT1 Channels by Stabilizing their Interaction with 14-3-3- Proteins.

Saponaro, Andrea ; Porro, Alessandro ; Chaves-Sanjuan, Antonio ; Nardini, Marco ; Rauh, Oliver ; Thiel, Gerhard ; Moroni, Anna (2017)
Fusicoccin Activates KAT1 Channels by Stabilizing their Interaction with 14-3-3- Proteins.
In: The Plant cell, 29 (10)
Artikel, Bibliographie

Kurzbeschreibung (Abstract)

Plants acquire potassium (K+) ions for cell growth and movement via regulated diffusion through K+ channels. Here we present crystallographic and functional data showing that the K+ inward rectifier KAT1 channel is regulated by 14-3-3 proteins and further modulated by the phytotoxin fusicoccin, in analogy to the H+-ATPase. We identified a 14-3-3 mode III binding site at the very C-terminus of KAT1 and co-crystallized it with tobacco 14-3-3 proteins to describe the protein complex at atomic detail. Validation of this interaction by electrophysiology shows that 14-3-3 binding augments KAT1 conductance by increasing the maximal current and by positively shifting the voltage-dependency of gating. Fusicoccin potentiates the 14-3-3 effect on KAT1 activity by stabilizing their interaction. Crystal structure of the ternary complex reveals a non-canonical binding site for the toxin that adopts a novel conformation, never described before. The structural insights underscore the adaptability of fusicoccin, predicting more potential targets than so far anticipated. The data furthermore advocate a common mechanism of regulation of the proton pump and a potassium channel, two essential elements in K+ uptake in plant cells.

Typ des Eintrags: Artikel
Erschienen: 2017
Autor(en): Saponaro, Andrea ; Porro, Alessandro ; Chaves-Sanjuan, Antonio ; Nardini, Marco ; Rauh, Oliver ; Thiel, Gerhard ; Moroni, Anna
Art des Eintrags: Bibliographie
Titel: Fusicoccin Activates KAT1 Channels by Stabilizing their Interaction with 14-3-3- Proteins.
Sprache: Englisch
Publikationsjahr: Oktober 2017
Titel der Zeitschrift, Zeitung oder Schriftenreihe: The Plant cell
Jahrgang/Volume einer Zeitschrift: 29
(Heft-)Nummer: 10
Kurzbeschreibung (Abstract):

Plants acquire potassium (K+) ions for cell growth and movement via regulated diffusion through K+ channels. Here we present crystallographic and functional data showing that the K+ inward rectifier KAT1 channel is regulated by 14-3-3 proteins and further modulated by the phytotoxin fusicoccin, in analogy to the H+-ATPase. We identified a 14-3-3 mode III binding site at the very C-terminus of KAT1 and co-crystallized it with tobacco 14-3-3 proteins to describe the protein complex at atomic detail. Validation of this interaction by electrophysiology shows that 14-3-3 binding augments KAT1 conductance by increasing the maximal current and by positively shifting the voltage-dependency of gating. Fusicoccin potentiates the 14-3-3 effect on KAT1 activity by stabilizing their interaction. Crystal structure of the ternary complex reveals a non-canonical binding site for the toxin that adopts a novel conformation, never described before. The structural insights underscore the adaptability of fusicoccin, predicting more potential targets than so far anticipated. The data furthermore advocate a common mechanism of regulation of the proton pump and a potassium channel, two essential elements in K+ uptake in plant cells.

ID-Nummer: pmid:28970335
Fachbereich(e)/-gebiet(e): 10 Fachbereich Biologie
10 Fachbereich Biologie > Plant Membrane Biophyscis (am 20.12.23 umbenannt in Biologie der Algen und Protozoen)
Hinterlegungsdatum: 18 Okt 2017 07:09
Letzte Änderung: 05 Dez 2017 13:45
PPN:
Export:
Suche nach Titel in: TUfind oder in Google
Frage zum Eintrag Frage zum Eintrag

Optionen (nur für Redakteure)
Redaktionelle Details anzeigen Redaktionelle Details anzeigen