Voltage-sensor transitions of the inward-rectifying K+ channel KAT1 indicate a latching mechanism biased by hydration within the voltage sensor.

@article{Lefoulon2014VoltagesensorTO,
  title={Voltage-sensor transitions of the inward-rectifying K+ channel KAT1 indicate a latching mechanism biased by hydration within the voltage sensor.},
  author={C{\'e}cile Lefoulon and Rucha Karnik and Annegret Honsbein and Paul Vijay Kanth Gutla and Christopher Grefen and Janin Riedelsberger and Tomas Poblete and Ingo Dreyer and Wendy Gonz{\'a}lez and Michael R Blatt},
  journal={Plant physiology},
  year={2014},
  volume={166 2},
  pages={
          960-75
        }
}
The Kv-like (potassium voltage-dependent) K(+) channels at the plasma membrane, including the inward-rectifying KAT1 K(+) channel of Arabidopsis (Arabidopsis thaliana), are important targets for manipulating K(+) homeostasis in plants. Gating modification, especially, has been identified as a promising means by which to engineer plants with improved characteristics in mineral and water use. Understanding plant K(+) channel gating poses several challenges, despite many similarities to that of… CONTINUE READING

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CITES BACKGROUND & METHODS
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References

Publications referenced by this paper.
SHOWING 1-10 OF 75 REFERENCES

Overexpression of plasma membrane H+-ATPase in guard cells promotes light-induced stomatal opening and enhances plant growth.

  • Proceedings of the National Academy of Sciences of the United States of America
  • 2014
VIEW 5 EXCERPTS
HIGHLY INFLUENTIAL

Distributed structures determine K + and voltage dependent gating of the Kin channel KAT 1 and the Kout channel SKOR

P Gajdanowicz, C Garcia-Mata, +7 authors I Dreyer
  • New Phytol
  • 2009
VIEW 10 EXCERPTS
HIGHLY INFLUENTIAL

K+-Sensitive Gating of the K+ Outward Rectifier in Vicia Guard Cells

  • The Journal of Membrane Biology
  • 1997
VIEW 4 EXCERPTS
HIGHLY INFLUENTIAL