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Capturing the phosphorylation and protein interaction landscape of the plant TOR kinase
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Capturing the phosphorylation and protein interaction landscape of the plant TOR kinase
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Journal Article
Capturing the phosphorylation and protein interaction landscape of the plant TOR kinase
2019
Overview
The target of rapamycin (TOR) kinase is a conserved regulatory hub that translates environmental and nutritional information into permissive or restrictive growth decisions. Despite the increased appreciation of the essential role of the TOR complex in plants, no large-scale phosphoproteomics or interactomics studies have been performed to map TOR signalling events in plants. To fill this gap, we combined a systematic phosphoproteomics screen with a targeted protein complex analysis in the model plant
Arabidopsis thaliana
. Integration of the phosphoproteome and protein complex data on the one hand shows that both methods reveal complementary subspaces of the plant TOR signalling network, enabling proteome-wide discovery of both upstream and downstream network components. On the other hand, the overlap between both data sets reveals a set of candidate direct TOR substrates. The integrated network embeds both evolutionarily-conserved and plant-specific TOR signalling components, uncovering an intriguing complex interplay with protein synthesis. Overall, the network provides a rich data set to start addressing fundamental questions about how TOR controls key processes in plants, such as autophagy, auxin signalling, chloroplast development, lipid metabolism, nucleotide biosynthesis, protein translation or senescence.
The target of rapamycin (TOR) kinase, present in all eukaryotes, is a major regulator of growth and metabolism. Using quantitative phosphoproteomics and comprehensive interactome approaches, the authors reveal the TOR signalling network, including potential substrates.
