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Mechanisms of regulation of SNF1/AMPK/SnRK1 protein kinases
Publication . Crozet, Pierre; Margalha, Leonor; Confraria, Ana; Rodrigues, Américo; Martinho, Cláudia; Adamo, Mattia; Elias, Carlos A.; Baena-González, Elena
The SNF1 (sucrose non-fermenting 1)-related protein kinases 1 (SnRKs1) are the plant orthologs of the budding yeast SNF1 and mammalian AMPK (AMP-activated protein kinase). These evolutionarily conserved kinases are metabolic sensors that undergo activation in response to declining energy levels. Upon activation, SNF1/AMPK/SnRK1 kinases trigger a vast transcriptional and metabolic reprograming that restores energy homeostasis and promotes tolerance to adverse conditions, partly through an induction of catabolic processes and a general repression of anabolism. These kinases typically function as a heterotrimeric complex composed of two regulatory subunits, β and γ, and an α-catalytic subunit, which requires phosphorylation of a conserved activation loop residue for activity. Additionally, SNF1/AMPK/SnRK1 kinases are controlled by multiple mechanisms that have an impact on kinase activity, stability, and/or subcellular localization. Here we will review current knowledge on the regulation of SNF1/AMPK/SnRK1 by upstream components, post-translational modifications, various metabolites, hormones, and others, in an attempt to highlight both the commonalities of these essential eukaryotic kinases and the divergences that have evolved to cope with the particularities of each one of these systems.
The Arabidopsis SR45 Splicing Factor, a Negative Regulator of Sugar Signaling, Modulates SNF1-Related Protein Kinase 1 Stability
Publication . Carvalho, Raquel F.; Szakonyi, Dóra; Simpson, Craig G.; Barbosa, Inês C.R.; Brown, John W.S.; Baena-González, Elena; Duque, Paula
The ability to sense and respond to sugar signals allows plants to cope with environmental and metabolic changes by adjusting growth and development accordingly. We previously reported that the SR45 splicing factor negatively regulates glucose signaling during early seedling development in Arabidopsis thaliana Here, we show that under glucose-fed conditions, the Arabidopsis sr45-1 loss-of-function mutant contains higher amounts of the energy-sensing SNF1-Related Protein Kinase 1 (SnRK1) despite unaffected SnRK1 transcript levels. In agreement, marker genes for SnRK1 activity are upregulated in sr45-1 plants, and the glucose hypersensitivity of sr45-1 is attenuated by disruption of the SnRK1 gene. Using a high-resolution RT-PCR panel, we found that the sr45-1 mutation broadly targets alternative splicing in vivo, including that of the SR45 pre-mRNA itself. Importantly, the enhanced SnRK1 levels in sr45-1 are suppressed by a proteasome inhibitor, indicating that SR45 promotes targeting of the SnRK1 protein for proteasomal destruction. Finally, we demonstrate that SR45 regulates alternative splicing of the Arabidopsis 5PTase13 gene, which encodes an inositol polyphosphate 5-phosphatase previously shown to interact with and regulate the stability of SnRK1 in vitro, thus providing a mechanistic link between SR45 function and the modulation of degradation of the SnRK1 energy sensor in response to sugars.
Shaping plant development through the SnRK1–TOR metabolic regulators
Publication . Baena-González, Elena; Hanson, Johannes
SnRK1 (Snf1-related protein kinase 1) and TOR (target ofrapamycin) are evolutionarily conserved protein kinases thatlie at the heart of energy sensing, playing central andantagonistic roles in the regulation of metabolism and geneexpression. Increasing evidence links these metabolicregulators to numerous aspects of plant development, fromgermination to flowering and senescence. This prompts thehypothesis that SnRK1 and TOR modify developmentalprograms according to the metabolic status to adjust plantgrowth to a specific environment. The aim of this review is toprovide support to this hypothesis and to incentivize furtherstudies on this topic by summarizing the work that establishesa genetic connection between SnRK1–TOR and plantdevelopment.

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Funding agency

Fundação para a Ciência e a Tecnologia

Funding programme

3599-PPCDT

Funding Award Number

PTDC/BIA-PLA/3937/2012

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