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High-affinity binding sites for abscisic acid on the plasmalemma of Vicia faba guard cells

Abstract

Stomata have a key role in the regulation of gas exchange and water economy in higher plants1,2. During water stress, they close in response to abscisic acid (ABA), a hormonal stimulus thought to be released or produced de novo in the mesophyll of leaves3,4, and probably in the guard cells of the stomata themselves5. By a mechanism still unknown, ABA affects the ionic balance of guard cells, resulting in a loss of K+, their major osmotically active constituent1,6. The structural requirements for a compound to be physiologically active in this system are stringent7 and suggest a highly specific interaction of the hormone with its primary target site(s). Apart from two preliminary studies8,9, ABA binding has not been investigated in plant material. Using guard cell protoplasts10,11, we have now obtained evidence for the occurrence of high-affinity guard cell-specific ABA-binding proteins which are located at the plasmalemma of these cells with high density. In all characteristics examined, they bear the properties of ABA receptors.

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Hornberg, C., Weiler, E. High-affinity binding sites for abscisic acid on the plasmalemma of Vicia faba guard cells. Nature 310, 321–324 (1984). https://doi.org/10.1038/310321a0

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