000 02729nam a2200241Ia 4500
003 MX-MdCICY
005 20250625124718.0
040 _cCICY
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
942 _2Loc
_cREF1
008 250602s9999 xx |||||s2 |||| ||und|d
999 _c42622
_d42622