A systems study reveals concurrent activation of AMPK and mTOR by amino acids

Dalle Pezze P, Ruf S, Sonntag AG, Langelaar-Makkinje M, Hall P, Heberle AM, Razquin Navas P, van Eunen K, Tölle RC, Schwarz JJ, Wiese H, Warscheid B · 2016 · Nature Communications · Atlas ID DAL2016

What this study shows

Adding amino acids back to starved cells switched on AMPK, PI3K and mTORC2 acutely and independently of mTORC1, at the same time as mTOR. AMPK activation ran through CaMKK-beta and, under amino acid sufficiency, AMPK kept autophagy going via ULK1. So the textbook picture of AMPK and mTORC1 as simple opposites does not hold in the first minutes after feeding - which matters for how the AMPK-ULK1 feedback arm behaves over time.

Abstract

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Amino acids (aa) are not only building blocks for proteins, but also signalling molecules, with the mammalian target of rapamycin complex 1 (mTORC1) acting as a key mediator. However, little is known about whether aa, independently of mTORC1, activate other kinases of the mTOR signalling network. To delineate aa-stimulated mTOR network dynamics, we here combine a computational-experimental approach with text mining-enhanced quantitative proteomics.

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At a glance

Evidence type	M Molecular — cells, biochemistry, structure Marked M because it is molecular or in-vitro work (model: Human cell lines; amino acid re-addition time courses, quantitative proteomics and dynamic modelling) rather than a whole-organism health-outcome study. That is often exactly where causal biology gets established -- the code says which system the finding was shown in, and nothing about how good the work is.
Study type	5 - Mechanistic / In Vitro
Model system	Human cell lines; amino acid re-addition time courses, quantitative proteomics and dynamic modelling
Journal	Nature Communications
Year	2016
Peer reviewed	Yes
Record last updated	2026-09-23
Source	DOI 10.1038/ncomms13254 · PMID 27869123 · Free full text (PMC5121333)

Extracted findings

Intervention	Amino acid withdrawal and re-addition
Target	AMPK; PI3K; mTORC2; mTORC1; ULK1
Model	Human cell lines
Effect	Amino acids acutely co-activate AMPK and mTOR; AMPK sustains autophagy under amino acid sufficiency

In the Atlas

Cite this paper

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Dalle Pezze, P., Ruf, S., Sonntag, A. G., Langelaar-Makkinje, M., Hall, P., Heberle, A. M., Razquin Navas, P., van Eunen, K., Tölle, R. C., Schwarz, J. J., Wiese, H., Warscheid, B., Deitersen, J., Stork, B., Fäßler, E., Schäuble, S., Hahn, U., Horvatovich, P., Shanley, D. P., & Thedieck, K. (2016). A systems study reveals concurrent activation of AMPK and mTOR by amino acids. Nature Communications. https://doi.org/10.1038/ncomms13254

@article{DAL2016,
  author       = {Dalle Pezze, P. and Ruf, S. and Sonntag, A. G. and Langelaar-Makkinje, M. and Hall, P. and Heberle, A. M. and Razquin Navas, P. and van Eunen, K. and Tölle, R. C. and Schwarz, J. J. and Wiese, H. and Warscheid, B. and Deitersen, J. and Stork, B. and Fäßler, E. and Schäuble, S. and Hahn, U. and Horvatovich, P. and Shanley, D. P. and Thedieck, K.},
  title        = {{A systems study reveals concurrent activation of AMPK and mTOR by amino acids}},
  journal      = {Nature Communications},
  year         = {2016},
  doi          = {10.1038/ncomms13254},
  note         = {PMID: 27869123},
}

Cite this Atlas record

The record is the Atlas's own work — the evidence label, the extracted findings and the links. It is cited as part of the dataset, not as the paper.

Barton, O. (2026). Oliver's mTOR Atlas (record DAL2016) [Data set]. https://mtor-atlas.org/study/DAL2016/ · Dataset DOI 10.5281/zenodo.22059963

@misc{atlas_DAL2016,
  author       = {Barton, Oliver},
  title        = {{Oliver's mTOR Atlas}, record DAL2016},
  howpublished = {Data set},
  year         = {2026},
  url          = {https://mtor-atlas.org/study/DAL2016/},
  doi          = {10.5281/zenodo.22059963}
}