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Impact of the SnRK1 protein kinase on sucrose homeostasis and the transcriptome during the diel cycle

ABSTRACT: Sucrose Non-Fermenting1-Related Kinase1 (SnRK1) is an evolutionarily conserved protein kinase with key functions in energy management during stress responses in plants. To address a potential role of SnRK1 under non-stress conditions, we performed a metabolomic and transcriptomic characterization of 20 d-old rosettes of Arabidopsis SnRK1 gain- and loss-of-function mutants during the diurnal cycle. SnRK1 manipulation altered the slope of the correlation between sucrose and trehalose 6-phosphate (Tre6P). It also modulated the flux of carbon to the tricarboxylic acid cycle downstream of Tre6P-signalling. SnRK1 depletion modified expression of SnRK1-induced genes least at the end of the day (when Tre6P levels peak) and most at the end of the night (when Tre6P levels are lowest). Expression of a subset of these genes was attenuated by inducible Tre6P accumulation in a time-of-day dependent manner. Finally, transcriptional profiling uncovered a wide impact of SnRK1 on gene expression in non-stress conditions, establishing a clear connection with iron and sulfur metabolism. In conclusion, SnRK1 plays central functions in metabolic and transcriptional regulation in the absence of stress. SnRK1 is further involved in the reciprocal control of sucrose-driven Tre6P production and/or degradation and its activity is modulated by daily fluctuations in Tre6P levels.

ORGANISM(S): Arabidopsis thaliana

PROVIDER: GSE168382 | GEO | 2021/06/01

REPOSITORIES: GEO

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Quantitative phosphoproteomics reveals SnRK1-dependent phosphosites in rice sheaths during grain filling

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Project description:Sucrose non-fermenting-1-related protein kinase 1 (SnRK1) is a central regulator of metabolism and developmental transition in plant. Compound 991 is a well-known 5′-adenosine monophosphate activated protein kinase (AMPK) activator in mammals. SnRK1 and AMPK are highly conserved. However, whether 991 could also act as a SnRK1 activator is unknown. Adding 991 significantly increased the activity of SnRK1 in desalted extracts from germinating rice seeds in vitro. To determine whether 991 has biological activity in plant, rice seeds were treated with different concentrations of 991. Low concentration of 991 promoted rice seed germination, while high concentration of 991 inhibited rice germination. The effect of 991 on rice germination is similar to the effect of OsSnRK1a overexpression on germination. To explore whether 991 affects germination by specifically affecting SnRK1, the germination status of the snrk1a mutant and WT under 1 μM 991 treatment were compared. The snrk1a mutant exhibited insensitivity to 991. Through phosphoproteomic analysis, we found that the differential phosphopeptides caused by 991 treatments and overexpression of OsSnRK1a are largely overlapped. Phosphoproteomic analysis also revealed that SnRK1 might affect rice germination by regulating the phosphorylation levels of S285-PIP2;4, S1013-SOS1 and S110-ABI5. These results showed that 991 is a specific and workable SnRK1 activator in rice. The promotion and inhibition of 991 treatments on germination also exist in wheat seeds. 991 is expected to be used for exploring the function of SnRK1 in more detail and depth and chemical regulation of growth and development in crops.

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Impact of the SnRK1 protein kinase on sucrose homeostasis and the transcriptome during the diel cycle

Project description:Impact of the SnRK1 protein kinase on sucrose homeostasis and the transcriptome during the diel cycle

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A Nitrogen-specific Interactome Analysis Sheds Light on the Role of the SnRK1 and TOR Kinases inPlant Nitrogen Signaling - part2 kinase assay

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Quantitative Phosphoproteomics Reveals Targets of Protein Kinase SnRK1 in Arabidopsis under Submergence

Project description:SNF1 RELATED PROTEIN KINASE 1 (SnRK1) is proposed as a central integrator of regulatory pathways in plant stress and energy starvation signaling. We observed in this study that the Arabidopsis SnRK1.1 dominant negative mutant (SnRK1.1K48M) had lower tolerance to submergence than the wild-type, suggesting that SnRK1.1-dependent phosphorylation of target proteins is important in energy starvation signaling triggered by submergence. To gain further insight into submergence signaling mechanisms, we determined the temporal response to energy starvation through AMP/ATP quantification and used quantitative phosphoproteomics to compare the global changes in phosphopeptides in Col-0 and SnRK1.1K48M. We found that the phosphorylation levels of 59 peptides increased and the levels of 96 peptides decreased in Col-0 within 0.5–3 h of submergence. Among the 59 peptides with increased phosphorylation in Col-0, 49 did not show increased phosphorylation levels in SnRK1.1K48M under submergence. These proteins are involved in sugar synthesis, glycolysis, osmotic regulation, ABA signaling, protein synthesis and ROS signaling. In particular, the phosphorylation of MAPK6, which is involved in regulating ROS responses under different abiotic stresses, was disrupted in the SnRK1.1K48M mutant. In addition, PTP1, a negative regulator of MAPK6 activity that directly dephosphorylates MAPK6, was also regulated by SnRK1.1. These results reveal insights into the function of SnRK1 and the downstream signaling factors of submergence.

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