| First Author | Humphrey SJ | Year | 2013 |
| Journal | Cell Metab | Volume | 17 |
| Issue | 6 | Pages | 1009-1020 |
| PubMed ID | 23684622 | Mgi Jnum | J:355640 |
| Mgi Id | MGI:6829084 | Doi | 10.1016/j.cmet.2013.04.010 |
| Citation | Humphrey SJ, et al. (2013) Dynamic adipocyte phosphoproteome reveals that Akt directly regulates mTORC2. Cell Metab 17(6):1009-1020 |
| abstractText | 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. |
