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      Properties of shaker-type potassium channels in higher plants.

      1 ,
      The Journal of membrane biology
      Springer Nature

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          Abstract

          Potassium (K(+)), the most abundant cation in biological organisms, plays a crucial role in the survival and development of plant cells, modulation of basic mechanisms such as enzyme activity, electrical membrane potentials, plant turgor and cellular homeostasis. Due to the absence of a Na(+)/K(+) exchanger, which widely exists in animal cells, K(+) channels and some type of K(+) transporters function as K(+) uptake systems in plants. Plant voltage-dependent K(+) channels, which display striking topological and functional similarities with the voltage-dependent six-transmembrane segment animal Shaker-type K(+) channels, have been found to play an important role in the plasma membrane of a variety of tissues and organs in higher plants. Outward-rectifying, inward-rectifying and weakly-rectifying K(+) channels have been identified and play a crucial role in K(+) homeostasis in plant cells. To adapt to the environmental conditions, plants must take advantage of the large variety of Shaker-type K(+) channels naturally present in the plant kingdom. This review summarizes the extensive data on the structure, function, membrane topogenesis, heteromerization, expression, localization, physiological roles and modulation of Shaker-type K(+) channels from various plant species. The accumulated results also help in understanding the similarities and differences in the properties of Shaker-type K(+) channels in plants in comparison to those of Shaker channels in animals and bacteria.

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          Author and article information

          Journal
          J. Membr. Biol.
          The Journal of membrane biology
          Springer Nature
          0022-2631
          0022-2631
          Mar 2006
          : 210
          : 1
          Affiliations
          [1 ] Istituto di Biofisica, Consiglio Nazionale delle Ricerche, Via De Marini 6, 16149 Genova, Italy. gambale@ge.ibf.cnr.it
          Article
          10.1007/s00232-006-0856-x
          16794778
          426b7756-e902-4c6e-82e3-3647d9bb62c7
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