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THE PLANT CELL, Vol 7, Issue 12 2197-2210, Copyright © 1995 by American Society of Plant Biologists
G Protein Activation Stimulates Phospholipase D Signaling in Plants
T. Munnik, S. A. Arisz, T. de Vrije and A. Musgrave
Institute for Molecular Cell Biology, BioCentrum Amsterdam, University of Amsterdam, Kruislaan 318, NL-1098 SM, Amsterdam, The Netherlands
We provide direct evidence for phospholipase D (PLD) signaling in plants by
showing that this enzyme is stimulated by the G protein activators
mastoparan, ethanol, and cholera toxin. An in vivo assay for PLD activity
in plant cells was developed based on the use of a "reporter alcohol"
rather than water as a transphosphatidylation substrate. The product was a
phosphatidyl alcohol, which, in contrast to the normal product phosphatidic
acid, is a specific measure of PLD activity. When 32P-labeled cells were
treated with 0.1% n-butanol, 32P-phosphatidyl butanol (32P-PtdBut) was
formed in a time-dependent manner. In cells treated with any of the three G
protein activators, the production of 32P-PtdBut was increased in a
dose-dependent manner. The G protein involved was pertussis toxin
insensitive. Ethanol could activate PLD but was itself consumed by PLD as
transphosphatidylation substrate. In contrast, secondary alcohols (e.g.,
sec-butyl alcohol) activated PLD but did not function as substrate, whereas
tertiary alcohols did neither. Although most of the experiments were
performed with the green alga Chlamydomonas eugametos, the relevance for
higher plants was demonstrated by showing that PLD in carnation petals
could also be activated by mastoparan. The results indicate that PLD
activation must be considered as a potential signal transduction mechanism
in plants, just as in animals.
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