Plant Physiology Preview
Published on September 20, 2002; 10.1104/pp.006080
Received March 21, 2002
Returned for revision April 23, 2002
Accepted June 12, 2002
Activation of Phospholipases C and D Is an Early Response to a Cold Exposure in Arabidopsis Suspension Cells
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
* Corresponding author; email: eric.ruelland{at}snv.jussieu.fr.
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.
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