Capturing the phosphorylation and protein interaction landscape of the plant TOR kinase.
Arabidopsis
/ growth & development
Arabidopsis Proteins
/ genetics
Cell Culture Techniques
Mass Spectrometry
/ methods
Phosphatidylinositol 3-Kinases
/ genetics
Phosphoproteins
/ metabolism
Phosphorylation
Plants, Genetically Modified
Protein Interaction Mapping
Ribosomal Protein S6 Kinases, 90-kDa
/ metabolism
Seedlings
/ metabolism
Signal Transduction
Journal
Nature plants
ISSN: 2055-0278
Titre abrégé: Nat Plants
Pays: England
ID NLM: 101651677
Informations de publication
Date de publication:
03 2019
03 2019
Historique:
received:
27
09
2018
accepted:
28
01
2019
pubmed:
6
3
2019
medline:
18
6
2019
entrez:
6
3
2019
Statut:
ppublish
Résumé
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.
Identifiants
pubmed: 30833711
doi: 10.1038/s41477-019-0378-z
pii: 10.1038/s41477-019-0378-z
doi:
Substances chimiques
Arabidopsis Proteins
0
Phosphoproteins
0
Phosphatidylinositol 3-Kinases
EC 2.7.1.-
TOR protein, Arabidopsis
EC 2.7.1.137
Ribosomal Protein S6 Kinases, 90-kDa
EC 2.7.11.1
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
316-327Commentaires et corrections
Type : CommentIn