TY - JOUR A1 - Gajdanowicz, Pawel A1 - Michard, Erwan A1 - Sandmann, Michael A1 - Rocha, Marcio A1 - Correa, Luiz Gustavo Guedes A1 - Ramirez-Aguilar, Santiago J. A1 - Gomez-Porras, Judith L. A1 - Gonzalez, Wendy A1 - Thibaud, Jean-Baptiste A1 - van Dongen, Joost T. A1 - Dreyer, Ingo T1 - Potassium (K plus ) gradients serve as a mobile energy source in plant vascular tissues JF - Proceedings of the National Academy of Sciences of the United States of America N2 - The essential mineral nutrient potassium (K(+)) is the most important inorganic cation for plants and is recognized as a limiting factor for crop yield and quality. Nonetheless, it is only partially understood how K(+) contributes to plant productivity. K(+) is used as a major active solute to maintain turgor and to drive irreversible and reversible changes in cell volume. K(+) also plays an important role in numerous metabolic processes, for example, by serving as an essential cofactor of enzymes. Here, we provide evidence for an additional, previously unrecognized role of K(+) in plant growth. By combining diverse experimental approaches with computational cell simulation, we show that K(+) circulating in the phloem serves as a decentralized energy storage that can be used to overcome local energy limitations. Posttranslational modification of the phloem-expressed Arabidopsis K(+) channel AKT2 taps this "potassium battery," which then efficiently assists the plasma membrane H(+)-ATPase in energizing the transmembrane phloem (re) loading processes. KW - channel gating KW - energy limiting condition KW - phloem reloading KW - posttranslational regulation KW - potassium channel Y1 - 2011 U6 - https://doi.org/10.1073/pnas.1009777108 SN - 0027-8424 VL - 108 IS - 2 SP - 864 EP - 869 PB - National Acad. of Sciences CY - Washington ER - TY - GEN A1 - Riedelsberger, Janin A1 - Dreyer, Ingo A1 - Gonzalez, Wendy T1 - Outward rectification of voltage-gated K+ channels evolved at least twice in life history T2 - Postprints der Universität Potsdam : Mathematisch-Naturwissenschaftliche Reihe N2 - Voltage-gated potassium (K+) channels are present in all living systems. Despite high structural similarities in the transmembrane domains (TMD), this K+ channel type segregates into at least two main functional categories-hyperpolarization-activated, inward-rectifying (Kin) and depolarization-activated, outward-rectifying (Kout) channels. Voltage-gated K+ channels sense the membrane voltage via a voltage-sensing domain that is connected to the conduction pathway of the channel. It has been shown that the voltage-sensing mechanism is the same in Kin and Kout channels, but its performance results in opposite pore conformations. It is not known how the different coupling of voltage-sensor and pore is implemented. Here, we studied sequence and structural data of voltage-gated K+ channels from animals and plants with emphasis on the property of opposite rectification. We identified structural hotspots that alone allow already the distinction between Kin and Kout channels. Among them is a loop between TMD S5 and the pore that is very short in animal Kout, longer in plant and animal Kin and the longest in plant Kout channels. In combination with further structural and phylogenetic analyses this finding suggests that outward-rectification evolved twice and independently in the animal and plant kingdom. T3 - Zweitveröffentlichungen der Universität Potsdam : Mathematisch-Naturwissenschaftliche Reihe - 521 KW - multiple sequence alignment KW - potassium channel KW - Arabidopsis thaliana KW - inward rectification KW - pacemaker channels KW - S4-S5 linker KW - sensor KW - expression KW - mechanism KW - activation Y1 - 2019 U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:kobv:517-opus4-409594 SN - 1866-8372 IS - 521 ER - TY - JOUR A1 - Held, Katrin A1 - Pascaud, Francois A1 - Eckert, Christian A1 - Gajdanowicz, Pawel A1 - Hashimoto, Kenji A1 - Corratge-Faillie, Claire A1 - Offenborn, Jan Niklas A1 - Lacombe, Benoit A1 - Dreyer, Ingo A1 - Thibaud, Jean-Baptiste A1 - Kudla, Jörg T1 - Calcium-dependent modulation and plasma membrane targeting of the AKT2 potassium channel by the CBL4/CIPK6 calcium sensor/protein kinase complex JF - Cell research N2 - Potassium (K(+)) channel function is fundamental to many physiological processes. However, components and mechanisms regulating the activity of plant K(+) channels remain poorly understood. Here, we show that the calcium (Ca(2+)) sensor CBL4 together with the interacting protein kinase CIPK6 modulates the activity and plasma membrane (PM) targeting of the K(+) channel AKT2 from Arabidopsis thaliana by mediating translocation of AKT2 to the PM in plant cells and enhancing AKT2 activity in oocytes. Accordingly, akt2, cbl4 and cipk6 mutants share similar developmental and delayed flowering phenotypes. Moreover, the isolated regulatory C-terminal domain of CIPK6 is sufficient for mediating CBL4- and Ca(2+)-dependent channel translocation from the endoplasmic reticulum membrane to the PM by a novel targeting pathway that is dependent on dual lipid modifications of CBL4 by myristoylation and palmitoylation. Thus, we describe a critical mechanism of ion-channel regulation where a Ca(2+) sensor modulates K(+) channel activity by promoting a kinase interaction-dependent but phosphorylation-independent translocation of the channel to the PM. KW - calcium sensor KW - protein kinase KW - potassium channel KW - signal transduction Y1 - 2011 U6 - https://doi.org/10.1038/cr.2011.50 SN - 1001-0602 VL - 21 IS - 7 SP - 1116 EP - 1130 PB - Nature Publ. Group CY - Shanghai ER -