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Transcriptional responses to cantharidin, a protein phosphatase inhibitor, in Arabidopsis thaliana reveal the involvement of multiple signal transduction pathways

Bajsa, Joanna, Pan, Zhiqiang, Duke, Stephen O.
Physiologia plantarum 2011 v.143 no.2 pp. 188
Arabidopsis thaliana, Epicauta, abscisic acid, apoptosis, auxins, cantharidin, cell differentiation, cell proliferation, enzyme inhibitors, ethylene, flagellin, gene expression, gene expression regulation, genes, hypersensitive response, leaves, phosphoprotein phosphatase, photosynthetically active radiation, protein kinases, receptors, seedlings, sensors, serine, signal transduction, threonine, transcriptome
Cantharidin is a natural compound isolated from the blister beetle (Epicauta spp.). It is a potent inhibitor of protein serine/threonine phosphatases (PPPs), especially PP2A and PP4. Protein phosphatases and kinases maintain a sensitive balance between dephosphorylated and phosphorylated forms of appropriate proteins, thereby playing important roles in signal transduction pathways and regulation of gene expression, cellular proliferation, cell differentiation, apoptosis and other processes. The foliage of 12-day-old Arabidopsis thaliana seedlings was treated with 200 μM (IC30) of the PPP inhibitor cantharidin, and the entire transcriptome profile was determined by microarray analysis at 2, 10 and 24 h after treatment. The transcription of approximately 10% (2577) of the 24 000 genes of Arabidopsis changed significantly (P ≤ 0.05 and signal log ratios: ≥1 or ≤−1) after treatment. Inhibition of PPPs significantly reduced transcription of genes associated with auxin and light signaling and induced expression of genes involved in the hypersensitive response and in flagellin and abscisic acid signaling. The great variety of up- and downregulated genes in this microarray experiment implied that cantharidin interfered with the activities of PPPs that interact directly or indirectly with receptors or are located near the beginning of signal transduction pathways. In many cases, PPPs interact with protein complexes of various receptors such as ethylene or light sensors localized in different cell compartments. They function as negative regulators modifying receptor functions, thus altering signaling that influences transcriptional responses.