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Plant Physiology 124 (2): 693-702

Copyright © 2000 by the American Society of Plant Physiologists.

Plant Physiol, October 2000, Vol. 124, pp. 693-702

Abscisic Acid Stimulation of Phospholipase D in the Barley Aleurone Is G-Protein-Mediated and Localized to the Plasma Membrane1

Sian Ritchie and Simon Gilroy*

Department of Biology, Pennsylvania State University, 208 Mueller Laboratory, University Park, Pennsylvania 16802

We have previously determined that phospholipase D (PLD) is activated by abscisic acid (ABA), and this activation is required for the ABA response of the cereal aleurone cell. In this study, ABA-stimulated PLD activity was reconstituted in vitro in microsomal membranes prepared from aleurone protoplasts. The transient nature (20 min) and degree (1.5- to 2-fold) of activation in vitro were similar to that measured in vivo. Stimulation by ABA was only apparent in the membrane fraction and was associated with a fraction enriched in plasma membrane. These results suggest that an ABA receptor system and elements linking it to PLD activation are associated with the aleurone plasma membrane. The activation of PLD in vitro by ABA was dependent on the presence of GTP. Addition of GTPgamma S transiently stimulated PLD in an ABA-independent manner, whereas treatment with GDPbeta S or pertussis toxin blocked the PLD activation by ABA. Application of pertussis toxin to intact aleurone protoplasts inhibited the ability of ABA to activate PLD as well as antagonizing the ability of ABA to down-regulate gibberellic acid-stimulated alpha -amylase production. All of these data support the hypothesis that ABA stimulation of PLD activity occurs at the plasma membrane and is mediated by G-protein activity.


1 This work was supported by a grant from the U.S. Department of Agriculture (to S.G.).

* Corresponding author; e-mail sxg12{at}psu.edu; fax 814-865-9131.

© 2000 American Society of Plant Physiologists

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