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Published on October 6, 2006; 10.1104/pp.106.087718


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Received August 1, 2006
Accepted September 6, 2006

AKIN{beta}{gamma} Contributes to SnRK1 Heterotrimeric Complexes and Interacts with Two Proteins Implicated in Plant Pathogen Resistance Through Its KIS/GBD Sequence

Lionel Gissot , Cécile Polge , Mathieu Jossier , Thomas Girin , Jean-Pierre Bouly , Martin Kreis , and Martine Thomas *

Institut de Biotechnologie des Plantes (IBP), UMR CNRS 8618, Bâtiment 630, Université Paris-Sud, F-91405 Orsay Cedex, France; Laboratoire de Biologie Cellulaire, Laboratoire Commun de Cytologie, INRA Versailles, RD10, Route de Saint Cyr, F-78026 Versailles cedex, France
Institut de Biotechnologie des Plantes (IBP), UMR CNRS 8618, Bâtiment 630, Université Paris-Sud, F-91405 Orsay Cedex, France

* Corresponding author; email: martine.thomas{at}ibp.u-psud.fr.

The SNF1/AMP-activated protein kinase subfamily plays a central role in metabolic responses to nutritional and environmental stresses. In yeast and mammals, the {beta}- and {gamma}-non catalytic subunits are respectively implicated in substrate specificity and subcellular localization, and regulation of the kinase activity. The atypical {beta}{gamma}-subunit have been previously described in maize, presenting at its N-terminal end a sequence related to the KIS domain specific to the {beta}-subunits (Lumbreras et al., 2001). The existence of two components SnRK complexes containing the {beta}{gamma} subunit and one SnRK kinase had been thus proposed.

In this work, we show that, despite its unusual features, the Arabidopsis thaliana homologue AKIN{beta}{gamma} clearly interacts with AKIN{beta} subunits in vitro and in vivo, suggesting its involvement in heterotrimeric complexes located both in cytoplasm and nucleus. Unexpectedly, a transcriptional analysis of AKIN{beta}{gamma} gene expression highlighted the implication of alternative splicing mechanisms in the regulation of AKIN{beta}{gamma} expression. A two-hybrid screen performed with AKIN{beta}{gamma} as bait, together with in planta Bimolecular Fluorescence Complementation (BiFC) experiments, suggest the existence of interactions in the cytosol between AKIN{beta}{gamma} and two LRR rich proteins related to pathogen resistance proteins. Interestingly this interaction occurs through the truncated KIS domain which corresponds exactly to a "Glycogen Binding Domain" (GBD) recently described in mammals and yeast. A phylogenetic study suggests that AKIN{beta}{gamma} 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.




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