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CELL BIOLOGY AND SIGNAL TRANSDUCTION

AKIN Contributes to SnRK1 Heterotrimeric Complexes and Interacts with Two Proteins Implicated in Plant Pathogen Resistance through Its KIS/GBD Sequence¹

Institut de Biotechnologie des Plantes, Unité Mixte de Recherche Centre National de la Recherche Scientifique 8618, Université Paris-Sud, F–91405 Orsay cedex, France (L.G., C.P., M.J., T.G., J.-P.B., M.K., M.T.); and Laboratoire de Biologie Cellulaire, Laboratoire Commun de Cytologie, Institut National de la Recherche Agronomique Versailles, RD10, F–78026 Versailles cedex, France (L.G.)

The sucrose nonfermenting-1 protein kinase (SNF1)/AMP-activated protein kinase subfamily plays a central role in metabolic responses to nutritional and environmental stresses. In yeast (Saccharomyces cerevisiae) and mammals, the - and -noncatalytic subunits are implicated in substrate specificity and subcellular localization, respectively, and regulation of the kinase activity. The atypical -subunit has been previously described in maize (Zea mays), presenting at its N-terminal end a sequence related to the KIS (kinase interacting sequence) domain specific to the -subunits (Lumbreras et al., 2001). The existence of two components, SNF1-related protein kinase (SnRK1) complexes containing the -subunit and one SnRK1 kinase, had been proposed. In this work, we show that, despite its unusual features, the Arabidopsis (Arabidopsis thaliana) homolog AKIN clearly interacts with AKIN-subunits in vitro and in vivo, suggesting its involvement in heterotrimeric complexes located in both cytoplasm and nucleus. Unexpectedly, a transcriptional analysis of AKIN gene expression highlighted the implication of alternative splicing mechanisms in the regulation of AKIN expression. A two-hybrid screen performed with AKIN as bait, together with in planta bimolecular fluorescence complementation experiments, suggests the existence of interactions in the cytosol between AKIN and two leucine-rich repeats related to pathogen resistance proteins. Interestingly, this interaction occurs through the truncated KIS domain that corresponds exactly to a GBD (glycogen-binding domain) recently described in mammals and yeast. A phylogenetic study suggests that AKIN-related proteins are restricted to the plant kingdom. Altogether, these data suggest the existence of plant-specific SnRK1 trimeric complexes putatively involved in a plant-specific function such as plant-pathogen interactions.

² Present address: Laboratoire de Physiologie Cellulaire Végétale, UMR5168, CEA-CNRS-INRA, Univ. Joseph Fourier, F–38054 Grenoble, France.

³ Present address: Laboratoire Intégration des fonctions nutritives, UMR Biochimie et Physiologie Moléculaire des Plantes, ENSA-M/INRA/CNRS/UM2, place Viala, F–34060 INRA Montpellier cedex 1, France.

⁴ Present address: Laboratoire de Physiologie Cellulaire et Moléculaire des Plantes, Université Paris 6, bâtiment Le Raphaël, 3 rue Galilée, F–94200 Ivry-sur-Seine, France.

The author responsible for distribution of materials integral to the findings presented in this article in accordance with the policy described in the Instructions for Authors (www.plantphysiol.org) is: Martine Thomas (martine.thomas{at}u-psud.fr).

www.plantphysiol.org/cgi/doi/10.1104/pp.106.087718

^* Corresponding author; e-mail martine.thomas{at}u-psud.fr; fax 33 01–69–15–34–24.

Received August 1, 2006; accepted September 6, 2006; published October 6, 2006.

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