The mTOR-regulated phosphoproteome reveals a mechanism of mTORC1-mediated inhibition of growth factor signaling

The mammalian target of rapamycin (mTOR) protein kinase is a master growth promoter that nucleates two complexes, mTORC1 and mTORC2. Despite the diverse processes controlled by mTOR, few substrates are known. We defined the mTOR-regulated phosphoproteome by quantitative mass spectrometry and characterized the primary sequence motif specificity of mTOR using positional scanning peptide libraries. We found that the phosphorylation response to insulin is largely mTOR dependent and that mTOR exhibits a unique preference for proline, hydrophobic, and aromatic residues at the +1 position.

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Hsu, P. P., et al. (2011). The mTOR-regulated phosphoproteome reveals a mechanism of mTORC1-mediated inhibition of growth factor signaling. Science. https://doi.org/10.1126/science.1199498

@article{HSU2011,
  author       = {Hsu, P. P. and Sabatini, D. M. and others},
  title        = {{The mTOR-regulated phosphoproteome reveals a mechanism of mTORC1-mediated inhibition of growth factor signaling}},
  journal      = {Science},
  year         = {2011},
  doi          = {10.1126/science.1199498},
  note         = {PMID: 21659604},
}

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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 HSU2011) [Data set]. https://mtor-atlas.org/study/HSU2011/ · Dataset DOI 10.5281/zenodo.22059963

@misc{atlas_HSU2011,
  author       = {Barton, Oliver},
  title        = {{Oliver's mTOR Atlas}, record HSU2011},
  howpublished = {Data set},
  year         = {2026},
  url          = {https://mtor-atlas.org/study/HSU2011/},
  doi          = {10.5281/zenodo.22059963}
}