TY  - JOUR
A1  - Skłodowski, Kamil
A1  - Riedelsberger, Janin
A1  - Raddatz, Natalia
A1  - Riadi, Gonzalo
A1  - Caballero, Julio
A1  - Chérel, Isabelle
A1  - Schulze, Waltraud
A1  - Graf, Alexander
A1  - Dreyer, Ingo
T1  - The receptor-like pseudokinase MRH1 interacts with the voltage-gated potassium channel AKT2
JF  - Scientific reports
N2  - The potassium channel AKT2 plays important roles in phloem loading and unloading. It can operate as inward-rectifying channel that allows H+-ATPase-energized K+ uptake. Moreover, through reversible post-translational modifications it can also function as an open, K+-selective channel, which taps a ‘potassium battery’, providing additional energy for transmembrane transport processes. Knowledge about proteins involved in the regulation of the operational mode of AKT2 is very limited. Here, we employed a large-scale yeast two-hybrid screen in combination with fluorescence tagging and null-allele mutant phenotype analysis and identified the plasma membrane localized receptor-like kinase MRH1/MDIS2 (AT4G18640) as interaction partner of AKT2. The phenotype of the mrh1-1 knockout plant mirrors that of akt2 knockout plants in energy limiting conditions. Electrophysiological analyses showed that MRH1/MDIS2 failed to exert any functional regulation on AKT2. Using structural protein modeling approaches, we instead gathered evidence that the putative kinase domain of MRH1/MDIS2 lacks essential sites that are indispensable for a functional kinase suggesting that MRH1/MDIS2 is a pseudokinase. We propose that MRH1/MDIS2 and AKT2 are likely parts of a bigger protein complex. MRH1 might help to recruit other, so far unknown partners, which post-translationally regulate AKT2. Additionally, MRH1 might be involved in the recognition of chemical signals.
Y1  - 2017
U6  - https://doi.org/10.1038/srep44611
SN  - 2045-2322
VL  - 7
PB  - Nature Publishing Group
CY  - London
ER  -