Abstract
Using the patch-clamp technique we discovered that the voltage dependent anion channels in the plasma membrane of guard cells are activated by a rise in cytoplasmic Ca2+ in the presence of nucleotides. Upon activation, these anion channels catalyse anion currents 10-20 times higher than in the inactivated state, thus shifting the plasma membrane from a K+ conducting state to an anion conducting state. Prolonged stimulation by depolarizing voltages results in the inactivation of the anion current (t1/2 = 10-12 s). We suggest that activation of the anion channel by Ca2+ and nucleotides is a key event in the regulation of salt efflux from guard cells during stomatal closure.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Adenosine Triphosphate / analogs & derivatives*
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Adenosine Triphosphate / metabolism
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Adenosine Triphosphate / pharmacology
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Calcium / pharmacology*
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Egtazic Acid / pharmacology
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Fabaceae / physiology
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Guanosine 5'-O-(3-Thiotriphosphate) / pharmacology*
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Ion Channels / drug effects
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Ion Channels / physiology*
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Membrane Potentials / drug effects
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Plant Cells
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Plant Physiological Phenomena*
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Plants, Medicinal
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Potassium Channels / drug effects
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Potassium Channels / physiology
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Protoplasts / physiology
Substances
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Ion Channels
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Potassium Channels
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adenosine 5'-O-(3-thiotriphosphate)
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Guanosine 5'-O-(3-Thiotriphosphate)
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Egtazic Acid
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Adenosine Triphosphate
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Calcium