标题:Capturing the phosphorylation and protein interaction landscape of the plant TOR kinase
作者:Van Leene, Jelle; Han, Chao; Gadeyne, Astrid; Eeckhout, Dominique; Matthijs, Caroline; Cannoot, Bernard; De Winne, Nancy; Persiau, Geert 更多
作者机构:[Van Leene, Jelle; Han, Chao; Gadeyne, Astrid; Eeckhout, Dominique; Matthijs, Caroline; Cannoot, Bernard; De Winne, Nancy; Persiau, Geert; Van de Slij 更多
通讯作者:De Jaeger, G;De Jaeger, G
通讯作者地址:[De Jaeger, G]Univ Ghent, Dept Plant Biotechnol & Bioinformat, Ghent, Belgium;[De Jaeger, G]VIB Ctr Plant Syst Biol, Ghent, Belgium.
来源:NATURE PLANTS
出版年:2019
卷:5
期:3
页码:316-327
DOI:10.1038/s41477-019-0378-z
摘要: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.
收录类别:SCOPUS;SCIE
WOS核心被引频次:1
Scopus被引频次:2
资源类型:期刊论文
原文链接:https://www.scopus.com/inward/record.uri?eid=2-s2.0-85062456556&doi=10.1038%2fs41477-019-0378-z&partnerID=40&md5=39f78af0367bc03dab3dc63d4a7f5f39
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