Phosphatidic acid activates a wound-activated MAPK in Glycine max.
Many plant species demonstrate a systemic increase in phosphatidic acid (PA) levels after being wounded (Lee et al., 1997). To understand the role of PA in wound signal transduction, we investigated if PA can activate protein kinases in soybean (Glycine max L.). We found that a MAPK is activated in soybean seedlings in both wounded and neighboring unwounded leaves. The wound-activated soybean kinase is specifically recognized by an antibody against the alfalfa MAPK, SIMK. When PA production is inhibited with n-butanol, an inhibitor of phospholipase D, the wound-induced activation of the MAPK is suppressed, suggesting that an elevation in PA levels is essential for its activation. Supporting this is the observation that exogenous PA activates the MAPK in suspension-cultured soybean cells. Activation of the 49 kDa MAPK occurs almost exclusively by PA, as other lipids are unable to or can only weakly activate the kinase. PA-induced activation of the MAPK is not a direct effect on the kinase but is mediated by upstream kinases. Our results suggest that PA acts as a second messenger in wound-induced MAPK signaling in plants.
Lee
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Division of Molecular Life Sciences, Pohang University of Science and Technology, Pohang, 790-784, Korea.
Hirt
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Lee
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D003429:Cross Reactions; D004789:Enzyme Activation; D020928:Mitogen-Activated Protein Kinases / Q000187:drug effects / Q000276:immunology / Q000378:metabolism*; D010712:Phosphatidic Acids / Q000494:pharmacology*; D010812:Physical Stimulation; D018515:Plant Leaves / Q000502:physiology*; D010940:Plant Proteins; D015290:Second Messenger Systems; D013025:Glycine max
D010712:Phosphatidic Acids; D010940:Plant Proteins; D020928:Mitogen-Activated Protein Kinases; C419564:salt stress-induced MAP kinase