The DOI matches its Crossref record; 35 of the 35 references it cites were found in a registry or an index.
Dynamic Adipocyte Phosphoproteome Reveals that Akt Directly Regulates mTORC2
Open accessAbstract
A major challenge of the post-genomics era is to define the connectivity of protein phosphorylation networks. Here, we quantitatively delineate the insulin signaling network in adipocytes by high-resolution mass spectrometry-based proteomics. These data reveal the complexity of intracellular protein phosphorylation. We identified 37,248 phosphorylation sites on 5,705 proteins in this single-cell type, with approximately 15% responding to insulin. We integrated these large-scale phosphoproteomics data using a machine learning approach to predict physiological substrates of several diverse insulin-regulated kinases. This led to the identification of an Akt substrate, SIN1, a core component of the mTORC2 complex. The phosphorylation of SIN1 by Akt was found to regulate mTORC2 activity in response to growth factors, revealing topological insights into the Akt/mTOR signaling network. The dynamic phosphoproteome described here contains numerous phosphorylation sites on proteins involved in diverse molecular functions and should serve as a useful functional resource for cell biologists.
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Cites
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Cited by
mTOR at the nexus of nutrition, growth, ageing and disease
Liu, G. Y., & Sabatini, D. M. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-019-0199-y · Cited by 2,737
Reprogramming of fatty acid metabolism in cancer
Koundouros, N., & Poulogiannis, G. (2020) · British Journal of Cancer · doi:10.1038/s41416-019-0650-z · Cited by 1,614
Biochemical and cellular properties of insulin receptor signalling
Haeusler, R. A., McGraw, T. E., & Accili, D. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.89 · Cited by 739
An atlas of substrate specificities for the human serine/threonine kinome
Johnson, J. L., Yaron, T. M., Huntsman, E. M., Kerelsky, A., Song, J., Regev, A., Lin, T.-Y., Liberatore, K., Cizin, D. M., Cohen, B. M., et al. (2023) · Nature · doi:10.1038/s41586-022-05575-3 · Cited by 728
Protein Phosphorylation: A Major Switch Mechanism for Metabolic Regulation
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Self-citation
Metadata
- Authors
- Humphrey, S. J., Yang, G., Yang, P., Fazakerley, D. J., Stöckli, J., Yang, J. Y., & James, D. E.
- Venue
- Cell Metabolism
- Publisher
- Elsevier BV
- Published
- 2013-06
- Volume
- 17
- Issue
- 6
- Pages
- 1009-1020
- ISSN
- 1550-4131 (ISSN-L)
- OpenAlex
- W2101771026
- Cited by
- 411
- References
- 35
- FWCI
- 12.37
- Type
- journal article
- Language
- en
- Open access
- hybrid
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- creativecommons.org/licenses/by/3.0/ (vor, 45 d)
- Funders
- National Health and Medical Research Council
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- Humphrey, S. J., Yang, G., Yang, P., Fazakerley, D. J., Stöckli, J., Yang, J. Y., & James, D. E. (2013). Dynamic Adipocyte Phosphoproteome Reveals that Akt Directly Regulates mTORC2. Cell Metabolism. https://doi.org/10.1016/j.cmet.2013.04.010
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