First published online September 20, 2002; 10.1104/pp.006080
Plant Physiol, October 2002, Vol. 130, pp. 999-1007
Activation of Phospholipases C and D Is an Early Response to a
Cold Exposure in Arabidopsis Suspension Cells1
Eric
Ruelland,*
Catherine
Cantrel,
Myriam
Gawer,
Jean-Claude
Kader, and
Alain
Zachowski
Groupe de Physiologie Cellulaire et Moléculaire des Plantes,
Université Pierre-et-Marie-Curie/Centre National de la Recherche
Scientifique, Unité Mixte de Recherche 7632, 75252 Paris cedex
05, France
The signaling events generated by a cold exposure are poorly known
in plants. We were interested in checking the possible activation of
enzymes of the phosphoinositide signaling pathway in response to a
temperature drop. In Arabidopsis suspension cells labeled with
33PO43 , a cold treatment induces
a rapid increase of phosphatidic acid (PtdOH) content. This production
was due to the simultaneous activation of phospholipase C (through
diacylglycerol kinase activity) and phospholipase D, as monitored by
the production of inositol triphosphate and of transphosphatidylation
product, respectively. Moreover, inhibitors of the phosphoinositide
pathway and of diacylglycerol kinase reduced PtdOH production. Enzyme
activation occurred immediately after cells were transferred to low
temperature. The respective contribution of both kind of phospholipases
in cold-induced production of PtdOH could be estimated. We created
conditions where phospholipids were labeled with
33PO43, but with ATP being
nonradioactive. In such conditions, the apparition of radioactive PtdOH
reflected PLD activity. Thus, we demonstrated that during a cold
stress, phospholipase D activity accounted for 20% of PtdOH
production. The analysis of composition in fatty acids of cold-produced
PtdOH compared with that of different phospholipids confirmed that
cold-induced PtdOH more likely derived mainly from phosphoinositides.
The addition of chemical reagents modifying calcium availability
inhibited the formation of PtdOH, showing that the cold-induced
activation of phospholipase pathways is dependent on a calcium entry.
1
This work was supported by the Ministère
de la Recherche, by the Centre National de la Recherche Scientifique,
and by the Université Pierre et Marie Curie.
*
Corresponding author; e-mail eric.ruelland{at}snv.jussieu.fr; fax
33-1-44-27-36-47.
© 2002 American Society of Plant Physiologists
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