phorbol/arabidopsis thaliana

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Generation of active oxygen in elicited cells of Arabidopsis thaliana is mediated by a NADPH oxidase-like enzyme.

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Suspension-cultured cells of Arabidopsis thaliana generated active oxygen species (AOS) (measured by luminol-dependent chemiluminescence) following challenge with the bacterial protein elicitor harpin or the protein kinase activator phorbol 12-myristate 13-acetate. These responses were blocked by

AtDGK2, a novel diacylglycerol kinase from Arabidopsis thaliana, phosphorylates 1-stearoyl-2-arachidonoyl-sn-glycerol and 1,2-dioleoyl-sn-glycerol and exhibits cold-inducible gene expression.

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Diacylglycerol kinase (DGK) phosphorylates diacylglycerol (DAG) to generate phosphatidic acid (PA). Both DAG and PA are implicated in signal transduction pathways. DGKs have been widely studied in animals, but their analysis in plants is fragmentary. Here, we report the cloning and biochemical

Modulation of the Arabidopsis KAT1 channel by an activator of protein kinase C in Xenopus laevis oocytes.

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The Arabidopsis thaliana K(+) channel KAT1 has been suggested to play a key role in the regulation of the aperture of stomatal pores on the surface of plant leaves. Calcium-dependent and calcium-independent signaling pathways are involved in abscisic acid-mediated regulation of guard cell turgidity.

In Vivo Imaging of Diacylglycerol at the Cytoplasmic Leaflet of Plant Membranes.

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Diacylglycerol (DAG) is an important intermediate in lipid biosynthesis and plays key roles in cell signaling, either as a second messenger itself or as a precursor of phosphatidic acid. Methods to identify distinct DAG pools have proven difficult because biochemical fractionation affects the pools,

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