TY  - JOUR
A1  - Nukarinen, Ella
A1  - Nägele, Thomas
A1  - Pedrotti, Lorenzo
A1  - Wurzinger, Bernhard
A1  - Mair, Andrea
A1  - Landgraf, Ramona
A1  - Börnke, Frederik
A1  - Hanson, Johannes
A1  - Teige, Markus
A1  - Baena-Gonzalez, Elena
A1  - Dröge-Laser, Wolfgang
A1  - Weckwerth, Wolfram
T1  - Quantitative phosphoproteomics reveals the role of the AMPK plant ortholog SnRK1 as a metabolic master regulator under energy deprivation
JF  - Scientific Reports
N2  - Since years, research on SnRK1, the major cellular energy sensor in plants, has tried to define its role in energy signalling. However, these attempts were notoriously hampered by the lethality of a complete knockout of SnRK1. Therefore, we generated an inducible amiRNA::SnRK1α2 in a snrk1α1 knock out background (snrk1α1/α2) to abolish SnRK1 activity to understand major systemic functions of SnRK1 signalling under energy deprivation triggered by extended night treatment. We analysed the in vivo phosphoproteome, proteome and metabolome and found that activation of SnRK1 is essential for repression of high energy demanding cell processes such as protein synthesis. The most abundant effect was the constitutively high phosphorylation of ribosomal protein S6 (RPS6) in the snrk1α1/α2 mutant. RPS6 is a major target of TOR signalling and its phosphorylation correlates with translation. Further evidence for an antagonistic SnRK1 and TOR crosstalk comparable to the animal system was demonstrated by the in vivo interaction of SnRK1α1 and RAPTOR1B in the cytosol and by phosphorylation of RAPTOR1B by SnRK1α1 in kinase assays. Moreover, changed levels of phosphorylation states of several chloroplastic proteins in the snrk1α1/α2 mutant indicated an unexpected link to regulation of photosynthesis, the main energy source in plants.
KW  - phosphoproteomics
KW  - SnRK1
KW  - energy deprivation
KW  - plants
Y1  - 2016
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-167638
VL  - 6
IS  - 31697
ER  -