AKINbg Contributes to SnRK1 Heterotrimeric Complexes and Interacts with Two Proteins Implicated in Plant Pathogen Resistance through Its KIS/GBD Sequence1 (Record no. 42622)

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control field 20250625124718.0
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Transcribing agency CICY
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Classification number (OCLC) (R) ; Classification number, CALL (RLIN) (NR) B-8317
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Title AKINbg Contributes to SnRK1 Heterotrimeric Complexes and Interacts with Two Proteins Implicated in Plant Pathogen Resistance through Its KIS/GBD Sequence1
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Volume/sequential designation Plant Physiology, 142(3), p.931-944, 2006
520 3# - SUMMARY, ETC.
Summary, etc. 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 b- and g-noncatalytic subunits are implicated in substrate specificity and subcellular localization, respectively, and regulation of the kinase activity. The atypical bg-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 b-subunits (Lumbreras et al., 2001). The existence of two components, SNF1-related protein kinase (SnRK1)complexes containing the bg-subunit and one SnRK1 kinase, had been proposed. In this work, we show that, despite its unusual features, the Arabidopsis (Arabidopsis thaliana)homolog AKINbg clearly interacts with AKINb-subunits in vitro and in vivo, suggesting its involvement in heterotrimeric complexes located in both cytoplasm and nucleus. Unexpectedly, a transcriptional analysis of AKINbg gene expression highlighted the implication of alternative splicing mechanisms in the regulation of AKINbg expression. A two-hybrid screen performed with AKINbg as bait, together with in planta bimolecular fluorescence complementation experiments, suggests the existence of interactions in the cytosol between AKINbg 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 AKINbg-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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Personal name Gissot, L.
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Personal name Polge, C.
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Personal name Jossier, M.
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Personal name Girin, T.
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Personal name Bouly, J.P.
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Personal name Kreis, M.
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Personal name Thomas, M.
856 40 - ELECTRONIC LOCATION AND ACCESS
Uniform Resource Identifier <a href="https://drive.google.com/file/d/15s77AOazI0wikHVLJfg0Pi91oFdCOAFy/view?usp=drivesdk">https://drive.google.com/file/d/15s77AOazI0wikHVLJfg0Pi91oFdCOAFy/view?usp=drivesdk</a>
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  Clasificación local     Ref1 CICY CICY Documento préstamo interbibliotecario 25.06.2025   B-8317 25.06.2025 25.06.2025 Documentos solicitados