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Free Content Protein phosphorylation is a prerequisite for intracellular Ca2+ release and ion channel control by nitric oxide and abscisic acid in guard cells

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Recent work has indicated that nitric oxide (NO) and its synthesis are important elements of signal cascades in plant–pathogen defence, and are a prerequisite for drought and abscisic acid (ABA) responses in Arabidopsis thaliana and Vicia faba guard cells. NO regulates inward-rectifying K+ channels and Cl channels of Vicia guard cells via intracellular Ca2+ release. However, its integration with related signals, including the actions of serine–threonine protein kinases, is less well defined. We report here that the elevation of cytosolic-free [Ca2+] ([Ca2+]i) mediated by NO in guard cells is reversibly inhibited by the broad-range protein kinase antagonists staurosporine and K252A, but not by the tyrosine kinase antagonist genistein. The effects of kinase antagonism translate directly to a loss of NO-sensitivity of the inward-rectifying K+ channels and background (Cl channel) current, and to a parallel loss in sensitivity of the K+ channels to ABA. These results demonstrate that NO-dependent signals can be modulated through protein phosphorylation upstream of intracellular Ca2+ release, and they implicate a target for protein kinase control in ABA signalling that feeds into NO-dependent Ca2+ release.
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Keywords: Cl− channel; K+ channel; Vicia faba stomatal guard cell; cytosolic-free Ca2+ concentration; inward-rectifying; oxidative stress; protein kinase

Document Type: Research Article

Affiliations: Inst. de Investigaciones Biologicas, Universidad Nacional de Mar del Plata, 7600 Mar del Plata Buenos Aires, Argentina

Publication date: August 1, 2005

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