The DOI matches its Crossref record; 48 of the 48 references it cites were found in a registry or an index.
mTORC1 Phosphorylation Sites Encode Their Sensitivity to Starvation and Rapamycin
Open accessAbstract
Not mTORCing: Inhibition of the protein kinase complex mTORC1 has potentially beneficial therapeutic affects that include inhibition of cancer and extension of life span. However, effects of its inhibition in vivo have sometimes been disappointing. One reason may be that the well-studied inhibitor of mTORC1, rapamycin, inhibits some effects of mTORC1 but not others. In line with this idea, Kang et al. ( 1236566 ) show that the effect of rapamycin depends on the substrate. Characteristics of the phosphorylation sites on various substrates caused them to be phosphorylated with different efficiency by mTORC1. The substrates that were most efficiently phosphorylated were resistant to inhibition of mTORC1. The results explain how various sites, sometimes within the same protein, can differ in their sensitivity to rapamycin.
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Cites
mTOR Signaling in Growth Control and Disease
Laplante, M., & Sabatini, D. M. (2012) · Cell · doi:10.1016/j.cell.2012.03.017 · Cited by 8,509
Self-citationAMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1
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Self-citationPhosphorylation of ULK1 (hATG1) by AMP-Activated Protein Kinase Connects Energy Sensing to Mitophagy
Egan, D. F., Shackelford, D. B., Mihaylova, M. M., Gelino, S., Kohnz, R. A., Mair, W., Vasquez, D. S., Joshi, A., Gwinn, D. M., Taylor, R., et al. (2011) · Science · doi:10.1126/science.1196371 · Cited by 2,600
Nutrient-dependent mTORC1 Association with the ULK1–Atg13–FIP200 Complex Required for Autophagy
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A mammalian protein targeted by G1-arresting rapamycin–receptor complex
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ULK-Atg13-FIP200 Complexes Mediate mTOR Signaling to the Autophagy Machinery
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Raptor, a Binding Partner of Target of Rapamycin (TOR), Mediates TOR Action
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Cited by
mTOR Signaling in Growth, Metabolism, and Disease
Saxton, R. A., & Sabatini, D. M. (2017) · Cell · doi:10.1016/j.cell.2017.02.004 · Cited by 7,555
Self-citationmTOR 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
Self-citationMTOR: a pharmacologic target for autophagy regulation
Kim, Y. C., & Guan, K.-L. (2015) · Journal of Clinical Investigation · doi:10.1172/jci73939 · Cited by 2,126
Rapamycin: one drug, many effects
Li, J., Kim, S. G., & Blenis, J. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.01.001 · Cited by 1,287
mTOR as a central hub of nutrient signalling and cell growth
Kim, J., & Guan, K.-L. (2019) · Nature Cell Biology · doi:10.1038/s41556-018-0205-1 · Cited by 1,072
Metadata
- Authors
- Kang, S. A., Pacold, M. E., Cervantes, C. L., Lim, D., Lou, H. J., Ottina, K., Gray, N. S., Turk, B. E., Yaffe, M. B., & Sabatini, D. M.
- Venue
- Science
- Published
- 2013-07-26
- Volume
- 341
- Issue
- 6144
- Pages
- 1236566-1236566
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W1510881494
- Cited by
- 431
- References
- 48
- FWCI
- 18.02
- Type
- journal article
- Language
- en
- Open access
- green
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- Kang, S. A., Pacold, M. E., Cervantes, C. L., Lim, D., Lou, H. J., Ottina, K., Gray, N. S., Turk, B. E., Yaffe, M. B., & Sabatini, D. M. (2013). mTORC1 Phosphorylation Sites Encode Their Sensitivity to Starvation and Rapamycin. Science. https://doi.org/10.1126/science.1236566
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