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Sci. STKE, 17 October 2000
Vol. 2000, Issue 54, p. tw7
[DOI: 10.1126/stke.2000.54.tw7]

EDITORS' CHOICE

PLANT BIOLOGY Abscisic Acid to Phospholipase D

Abstract:

Ritchie and Gilroy developed an in vitro system to test whether abscisic acid (ABA) activates phospholipase D (PLD) in cereal aleurone cells through a heterotrimeric G protein (G protein). Stimulation of PLD activity by ABA was inhibited by GDP-ß-S and enhanced by GTP-{gamma}-S, consistent with the involvement of a G protein. Further support for a G protein came from the experiments performed in the presence of pertussis toxin, which inhibited ABA-stimulated PLD activity in vitro and in vivo. Membrane fractionation studies suggest that the ABA signaling pathway and the ABA-regulated PLD is associated with the plasma membrane. Thus, on the basis of results from this in vitro system, ABA activates a plasma membrane receptor that couples to a G protein, which leads to the regulation of a plasma membrane-localized PLD.

Ritchie, S., and Gilroy, S. (2000) Abscisic acid stimulation of phospholipase D in the barley aleurone is G-protein-mediated and localized to the plasma membrane. Plant Physiol. 124: 693-702. [Abstract] [Full Text]

Citation: Abscisic Acid to Phospholipase D. Sci. STKE 2000, tw7 (2000).

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Science Signaling. ISSN 1937-9145 (pre-2008: Science's STKE. ISSN 1525-8882)