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| 003 | MX-MdCICY | ||
| 005 | 20250625124718.0 | ||
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| 090 | _aB-8317 | ||
| 245 | 1 | 0 | _aAKINbg Contributes to SnRK1 Heterotrimeric Complexes and Interacts with Two Proteins Implicated in Plant Pathogen Resistance through Its KIS/GBD Sequence1 |
| 490 | 0 | _vPlant Physiology, 142(3), p.931-944, 2006 | |
| 520 | 3 | _aThe 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. | |
| 700 | 1 | 2 | _aGissot, L. |
| 700 | 1 | 2 | _aPolge, C. |
| 700 | 1 | 2 | _aJossier, M. |
| 700 | 1 | 2 | _aGirin, T. |
| 700 | 1 | 2 | _aBouly, J.P. |
| 700 | 1 | 2 | _aKreis, M. |
| 700 | 1 | 2 | _aThomas, M. |
| 856 | 4 | 0 |
_uhttps://drive.google.com/file/d/15s77AOazI0wikHVLJfg0Pi91oFdCOAFy/view?usp=drivesdk _zPara ver el documento ingresa a Google con tu cuenta: @cicy.edu.mx |
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