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Elicitor-Activated Phospholipase A₂ Generates Lysophosphatidylcholines That Mobilize the Vacuolar H⁺ Pool for pH Signaling via the Activation of Na⁺-Dependent Proton Fluxes

Institute of Pharmaceutical Biology, Department of Cell Physiology, Martin-Luther-University, 06120 Halle, Germany

¹ To whom correspondence should be addressed. E-mail roos{at}pharmazie.uni-halle.de; fax 49-345-5527006

The elicitation of phytoalexin biosynthesis in cultured cells of California poppy involves a shift of cytoplasmic pH via the transient efflux of vacuolar protons. Intracellular effectors of vacuolar proton transport were identified by a novel in situ approach based on the selective permeabilization of the plasma membrane for molecules of 10 kD. Subsequent fluorescence imaging of the vacuolar pH correctly reported experimental changes of activity of the tonoplast proton transporters. Lysophosphatidylcholine (LPC) caused a transient increase of the vacuolar pH by increasing the Na⁺ sensitivity of a Na⁺-dependent proton efflux that was inhibited by amiloride. In intact cells, yeast elicitor activated phospholipase A₂, as demonstrated by the formation of LPC from fluorescent substrate analogs, and caused a transient increase of endogenous LPC, as determined by matrix-assisted laser desorption and ionization time-of-flight mass spectrometry. It is suggested that LPC generated by phospholipase A₂ at the plasma membrane transduces the elicitor-triggered signal into the activation of a tonoplast H⁺/Na⁺ antiporter.

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