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Capturing the phosphorylation and protein interaction landscape of the plant TOR kinase

Jelle Van Leene (UGent) , Chao Han (UGent) , Astrid Gadeyne (UGent) , Dominique Eeckhout (UGent) , Caroline Matthijs, Bernard Cannoot (UGent) , Nancy De Winne (UGent) , Geert Persiau (UGent) , Eveline Van De Slijke (UGent) , Brigitte Van De Cotte (UGent) , et al.
(2019) NATURE PLANTS. 5(3). p.316-327
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Abstract
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.
Keywords
interactome, phosphoproteome, plants, Arabidopsis, target of rapamycin, kinase signaling

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Citation

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MLA
Van Leene, Jelle, et al. “Capturing the Phosphorylation and Protein Interaction Landscape of the Plant TOR Kinase.” NATURE PLANTS, vol. 5, no. 3, 2019, pp. 316–27, doi:10.1038/s41477-019-0378-z.
APA
Van Leene, J., Han, C., Gadeyne, A., Eeckhout, D., Matthijs, C., Cannoot, B., … De Jaeger, G. (2019). Capturing the phosphorylation and protein interaction landscape of the plant TOR kinase. NATURE PLANTS, 5(3), 316–327. https://doi.org/10.1038/s41477-019-0378-z
Chicago author-date
Van Leene, Jelle, Chao Han, Astrid Gadeyne, Dominique Eeckhout, Caroline Matthijs, Bernard Cannoot, Nancy De Winne, et al. 2019. “Capturing the Phosphorylation and Protein Interaction Landscape of the Plant TOR Kinase.” NATURE PLANTS 5 (3): 316–27. https://doi.org/10.1038/s41477-019-0378-z.
Chicago author-date (all authors)
Van Leene, Jelle, Chao Han, Astrid Gadeyne, Dominique Eeckhout, Caroline Matthijs, Bernard Cannoot, Nancy De Winne, Geert Persiau, Eveline Van De Slijke, Brigitte Van De Cotte, Elisabeth Stes, Michiel Van Bel, Veronique Storme, Francis Impens, Kris Gevaert, Klaas Vandepoele, Ive De Smet, and Geert De Jaeger. 2019. “Capturing the Phosphorylation and Protein Interaction Landscape of the Plant TOR Kinase.” NATURE PLANTS 5 (3): 316–327. doi:10.1038/s41477-019-0378-z.
Vancouver
1.
Van Leene J, Han C, Gadeyne A, Eeckhout D, Matthijs C, Cannoot B, et al. Capturing the phosphorylation and protein interaction landscape of the plant TOR kinase. NATURE PLANTS. 2019;5(3):316–27.
IEEE
[1]
J. Van Leene et al., “Capturing the phosphorylation and protein interaction landscape of the plant TOR kinase,” NATURE PLANTS, vol. 5, no. 3, pp. 316–327, 2019.
@article{8606506,
  abstract     = {{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.}},
  author       = {{Van Leene, Jelle and Han, Chao and Gadeyne, Astrid and Eeckhout, Dominique and Matthijs, Caroline and Cannoot, Bernard and De Winne, Nancy and Persiau, Geert and Van De Slijke, Eveline and Van De Cotte, Brigitte and Stes, Elisabeth and Van Bel, Michiel and Storme, Veronique and Impens, Francis and Gevaert, Kris and Vandepoele, Klaas and De Smet, Ive and De Jaeger, Geert}},
  issn         = {{2055-0278}},
  journal      = {{NATURE PLANTS}},
  keywords     = {{interactome,phosphoproteome,plants,Arabidopsis,target of rapamycin,kinase signaling}},
  language     = {{eng}},
  number       = {{3}},
  pages        = {{316--327}},
  title        = {{Capturing the phosphorylation and protein interaction landscape of the plant TOR kinase}},
  url          = {{http://doi.org/10.1038/s41477-019-0378-z}},
  volume       = {{5}},
  year         = {{2019}},
}
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