The Arabidopsis thaliana inward-rectifier K(+) channel AKT1 plays an important role in root K(+) uptake. Recent results show that the calcineurin B-like (CBL)-interacting protein kinase (CIPK) 23-CBL1/9 complex activates AKT1 in the root to enhance K(+) uptake. In addition, this CIPK-CBL complex has been demonstrated to regulate stomatal movements and plant transpiration. However, a role for AKT1 in plant transpiration has not yet been demonstrated. Here we show that disruption of AKT1 conferred an enhanced response to water stress in plants. Experiments performed in hydroponics showed that, when water potential was diminished by adding polyethylene glycol, akt1 adult plants lost less water than wild-type (WT) plants. Under long-term water stress in soil, adult akt1 plants displayed lower transpiration and less water consumption than WT plants. Finally, akt1 stomata closed more efficiently in response to ABA. Such results were also observed in cipk23 plants. The similar responses shown by cipk23 and akt1 plants to water stress denote that the regulation of AKT1 by CIPK23 may also take place in stomata and has a negative impact on plant performance under water stress conditions.
K(+) acquisition by Arabidopsis roots is mainly mediated by the high-affinity K(+) transporter AtHAK5 and the inward-rectifier K(+) channel AtAKT1. This model is probably universal to plants. Mutant plants lacking these two systems (athak5,atakt1) take up K(+) and grow when the external K(+) concentration is above a certain level, indicating that an additional transport system may compensate for the absence of AtHAK5 and AtAKT1. Here we describe that this alternative system is essential for providing sufficient K(+) to sustain growth of athak5,atakt1 plants. This system is especially sensitive to Ca(2+), Mg(2+), Ba(2+) and La(3+), it transports Cs(+) and its activity is reduced by cyclic nucleotides. These results suggest that a Ca(2+)-permeable voltage-independent non-selective cation channel, probably belonging to the cyclic nucleotide gated channel (CNGC) family, may provide the pathway for K(+) uptake in athak5,atakt1 plants. The genes encoding the two members of the CNGC family that have been described as mediating root K(+) uptake, AtCNGC3 and AtCNGC10, are not up-regulated in athak5,atakt1 plants, excluding overexpression of these genes as a compensatory mechanism. On the other hand, an increased driving force for K(+) in athak5,atakt1 plants due to a hyperpolarization of the membrane potential of its root cells is also discarded. The identification of this unknown system may provide tools to improve plant K(+) nutrition in conditions where AtAKT1 functionality is reduced, such as under salinity. In addition, this system may constitute an important pathway for accumulation of toxic cations such as Cs(+) or radiocesium ((137)Cs(+)), and could play a role in phytoremediation.
Potassium (K+) is an essential macronutrient required for plant growth, development and high yield production of crops. Members of group I of the KT/HAK/KUP family of transporters, such as HAK5, are key components for K+ acquisition by plant roots at low external K+ concentrations. Certain abiotic stress conditions such as salinity or Cs+-polluted soils may jeopardize plant K+ nutrition because HAK5-mediated K+ transport is inhibited by Na+ and Cs+. Here, by screening in yeast a randomly-mutated collection of AtHAK5 transporters, a new mutation in AtHAK5 sequence is identified that greatly increases Na+ tolerance. The single point mutation F130S, affecting an amino acid residue conserved in HAK5 transporters from several species, confers high salt tolerance, as well as Cs+ tolerance. This mutation increases more than 100-fold the affinity of AtHAK5 for K+ and reduces the Ki values for Na+ and Cs+, suggesting that the F130 residue may contribute to the structure of the pore region involved in K+ binding. In addition, this mutation increases the Vmax for K+. All this changes occur without increasing the amount of the AtHAK5 protein in yeast and support the idea that this residue is contributing to shape the selectivity filter of the AtHAK5 transporter.
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