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The receptor-like pseudokinase MRH1 interacts with the voltage-gated potassium channel AKT2.

Sci Rep. 2017 Mar 16;7:44611
Kamil Sklodowski 1 , Janin Riedelsberger 2 , Natalia Raddatz 3 , Gonzalo Riadi 2 , Julio Caballero 2 , Isabelle Chérel 4 , Waltraud Schulze 5 , Alexander Graf 6 , Ingo Dreyer 7
Kamil Sklodowski 1 , Janin Riedelsberger 2 , Natalia Raddatz 3 , Gonzalo Riadi 2 , Julio Caballero 2 , Isabelle Chérel 4 , Waltraud Schulze 5 , Alexander Graf 6 , Ingo Dreyer 7
+ et al

[No authors listed]

Author information
  • 1 ETH Zürich, Department of Biology, CH-8092 Zürich, Switzerland.
  • 2 Centro de Bioinformática y Simulación Molecular, Facultad de Ingeniería, Universidad de Talca, Talca, Chile.
  • 3 Instituto de Biología Vegetal y Fotosíntesis, Consejo Superior de Investigaciones Científicas, E-41092 Sevilla, Spain.
  • 4 Biochimie et Physiologie Moléculaire des Plantes, Centre National de la Recherche Scientifique Unité Mixte de Recherche 5004, Institut National de la Recherche Agronomique U386, Montpellier SupAgro, Université Montpellier II, F-34060 Montpellier cedex 2, France.
  • 5 Department of Plant Systems Biology, University of Hohenheim, D-70593 Stuttgart, Germany.
  • 6 Max-Planck-Institute of Molecular Plant Physiology, D-14476 Potsdam-Golm, Germany.
  • 7 Plant Biophysics, Centro de Biotecnología y Genómica de Plantas, Universidad Politécnica de Madrid (UPM) - Instituto Nacional de Investigación y Tecnología Agraria y Alimentaria (INIA), E-28223 Pozuelo de Alarcón (Madrid), Spain.

摘要


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.