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Published on September 3, 2008; 10.1104/pp.108.124594

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Received June 11, 2008
Accepted August 26, 2008

Protein tyrosine kinases and protein tyrosine phosphatases are involved in ABA-dependent processes in Arabidopsis thaliana seeds and suspension cells

Thanos Ghelis *, Gerard Bolbach , Gilles Clodic , Yvette Habricot , Emile Miginiac , Bruno Sotta , and Emmanuelle Jeannette

UPMC Universite Paris 06, UMR 7180, Laboratoire de Physiologie Cellulaire et Moleculaire des Plantes, 3 rue Galilee, 94200, Ivry sur Seine, France; CNRS, UMR 7180, Laboratoire de Physiologie Cellulaire et Moleculaire des Plantes, 3 rue Galilee, 94200, Ivry sur Seine, France; UPMC Universite Paris 06, IFR 83, Plate-Forme de Spectrometrie de Masse et Proteomique, 4 place Jussieu, 75005, Paris, France; CNRS, UMR 7613, Laboratoire de Structure et Fonction de Molecules Bioactives, 4 place Jussieu, 75005, Paris, France

* Corresponding author; email: thanos.ghelis{at}upmc.fr.

Protein tyrosine phosphorylation plays a central role in many signaling pathways leading to cell growth and differentiation in animals. Tyrosine phosphorylated proteins have been detected in higher plants and the roles of protein tyrosine phosphatases (PTPs) and protein tyrosine kinases (PTKs) in some physiological responses have been shown. We investigated the involvement of tyrosine phosphorylation events in abscisic acid (ABA) signaling using a pharmacological approach. Phenylarsine oxide (PAO), a specific inhibitor of PTP activity, abolished the ABA-dependent accumulation of RAB18 transcripts. PTK inhibitors like genistein, tyrphostin A23 and erbstatin, blocked the RAB18 expression induced by ABA in Arabidopsis. Stomatal closure induced by ABA was also inhibited by PAO and genistein. We studied the changes in the tyrosine phosphorylation levels of proteins in Arabidopsis seeds after ABA treatment. Proteins were separated by two-dimensional gel electrophoresis and those phosphorylated on tyrosine residues were detected using an anti-phosphotyrosine antibody by Western blot. Changes were detected in the tyrosine phosphorylation levels of 19 proteins after ABA treatment. Genistein inhibited the ABA-dependent tyrosine phosphorylation of proteins. The 19 proteins were analysed by MALDI-TOF-TOF mass spectrometry. Among the proteins identified were storage proteins like cruciferins, enzymes involved in the mobilization of lipid reserves like aconitase, enolase, aldolase and a lipoprotein, and enzymes necessary for seedling development like the large subunit of Rubisco. Additionally, the identification of three putative signaling proteins: a peptidyl-prolyl isomerase, a RNA-binding protein and a Small Ubiquitin-like MOdifier (SUMO) conjugating enzyme, enlightens how tyrosine phosphorylation might regulate ABA transduction pathways in plants.






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