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 |
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