Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.


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

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-β-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).


To Advertise     Find Products


Science Signaling. ISSN 1937-9145 (online), 1945-0877 (print). Pre-2008: Science's STKE. ISSN 1525-8882