Publication Information
Van Leene et al., 2019
Abstract
Nat Plants. 2019 Mar;5(3):316-327. doi: 10.1038/s41477-019-0378-z. Epub 2019 Mar
4.
Capturing the phosphorylation and protein interaction landscape of the plant TOR
kinase.
Van Leene J(1)(2), Han C(1)(2)(3), Gadeyne A(1)(2), Eeckhout D(1)(2), Matthijs
C(1)(2), Cannoot B(1)(2), De Winne N(1)(2), Persiau G(1)(2), Van De Slijke
E(1)(2), Van de Cotte B(1)(2), Stes E(1)(2), Van Bel M(1)(2)(4), Storme V(1)(2),
Impens F(5)(6)(7), Gevaert K(5)(6)(7), Vandepoele K(1)(2)(4), De Smet I(1)(2),
De Jaeger G(8)(9).
Author information:
(1)Department of Plant Biotechnology and Bioinformatics, Ghent University,
Ghent, Belgium.
(2)VIB Center for Plant Systems Biology, Ghent, Belgium.
(3)The Key Laboratory of Plant Cell Engineering and Germplasm Innovation,
College of Life Sciences, Shandong University, Jinan, China.
(4)Bioinformatics Institute Ghent, Ghent University, Ghent, Belgium.
(5)Department of Biochemistry, Ghent University, Ghent, Belgium.
(6)VIB Center for Medical Biotechnology, Ghent, Belgium.
(7)VIB Proteomics Core, Ghent, Belgium.
(8)Department of Plant Biotechnology and Bioinformatics, Ghent University,
Ghent, Belgium. geert.dejaeger@psb.vib-ugent.be.
(9)VIB Center for Plant Systems Biology, Ghent, Belgium.
geert.dejaeger@psb.vib-ugent.be.
Comment in
Nat Plants. 2019 Mar;5(3):251-252.
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.
DOI: 10.1038/s41477-019-0378-z
PMID: 30833711 [Indexed for MEDLINE]
