The DOI matches its Crossref record; 79 of the 79 references it cites were found in a registry or an index.
Quantitative phosphoproteomics reveals the role of the AMPK plant ortholog SnRK1 as a metabolic master regulator under energy deprivation
Open accessAbstract
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.
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Cited by
AMPK and TOR: The Yin and Yang of Cellular Nutrient Sensing and Growth Control
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Differential TOR activation and cell proliferation in Arabidopsis root and shoot apexes
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Broeckx, T., Hulsmans, S., & Rolland, F. (2016) · Journal of Experimental Botany · doi:10.1093/jxb/erw416 · Cited by 267
Capturing the phosphorylation and protein interaction landscape of the plant TOR kinase
Van Leene, J., Han, C., Gadeyne, A., Eeckhout, D., Matthijs, C., Cannoot, B., De Winne, N., Persiau, G., Van De Slijke, E., Van de Cotte, B., et al. (2019) · Nature Plants · doi:10.1038/s41477-019-0378-z · Cited by 266
Metadata
- Authors
- Nukarinen, E., Nägele, T., Pedrotti, L., Wurzinger, B., Mair, A., Landgraf, R., Börnke, F., Hanson, J., Teige, M., Baena-Gonzalez, E., Dröge-Laser, W., & Weckwerth, W.
- Venue
- Scientific Reports
- Published
- 2016-08-22
- Volume
- 6
- Issue
- 1
- Pages
- 31697-31697
- ISSN
- 2045-2322 (ISSN-L)
- OpenAlex
- W2511143602
- Cited by
- 334
- References
- 79
- FWCI
- 33.49
- Type
- journal article
- Language
- en
- Open access
- gold
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- Nukarinen, E., Nägele, T., Pedrotti, L., Wurzinger, B., Mair, A., Landgraf, R., Börnke, F., Hanson, J., Teige, M., Baena-Gonzalez, E., Dröge-Laser, W., & Weckwerth, W. (2016). Quantitative phosphoproteomics reveals the role of the AMPK plant ortholog SnRK1 as a metabolic master regulator under energy deprivation. Scientific Reports. https://doi.org/10.1038/srep31697
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