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

Sergei Sokolovski, Adrian Hills, Rob Gay, Carlos Garcia-Mata, Lorenzo Lamattina, Michael R. Blatt*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

Abstract

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.

Original languageEnglish
Pages (from-to)520-529
Number of pages10
JournalPlant Journal
Volume43
Issue number4
DOIs
Publication statusPublished - Aug 2005

Keywords

  • Cl channel
  • Cytosolic-free Ca concentration
  • Inward-rectifying
  • K channel
  • Oxidative stress
  • Protein kinase
  • Vicia faba stomatal guard cell

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