The DOI matches its Crossref record; 73 of the 73 references it cites were found in a registry or an index.
Characterization of Rictor Phosphorylation Sites Reveals Direct Regulation of mTOR Complex 2 by S6K1
Open accessAbstract
The mammalian target of rapamycin (mTOR) functions within two distinct complexes (mTORC1 and mTORC2) to control cell growth, proliferation, survival, and metabolism. While there has been great progress in our understanding of mTORC1 regulation, the signaling mechanisms that regulate mTORC2 have not been defined. In this study, we use liquid chromatography-tandem mass spectrometry analyses to identify 21 phosphorylation sites on the core mTORC2 component Rictor. We find that one site, T1135, undergoes growth factor-responsive phosphorylation that is acutely sensitive to rapamycin and is phosphorylated downstream of mTORC1. We find that Rictor-T1135 is directly phosphorylated by the mTORC1-dependent kinase S6K1. Although this phosphorylation event does not affect mTORC2 integrity or in vitro kinase activity, expression of a phosphorylation site mutant of Rictor (T1135A) in either wild-type or Rictor null cells causes an increase in the mTORC2-dependent phosphorylation of Akt on S473. However, Rictor-T1135 phosphorylation does not appear to regulate mTORC2-mediated effects on SGK1 or PKC alpha. While the precise molecular mechanism affecting Akt is unknown, phosphorylation of T1135 stimulates binding of Rictor to 14-3-3 proteins. We provide evidence that Rictor-T1135 phosphorylation acts in parallel with other mTORC1-dependent feedback mechanisms, such as those affecting IRS-1 signaling to PI3K, to regulate the response of Akt to insulin.
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Cites
Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex
Sarbassov, D. D., Guertin, D. A., Ali, S. M., & Sabatini, D. M. (2005) · Science · doi:10.1126/science.1106148 · Cited by 6,216
TOR signaling in growth and metabolism
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TSC2 is phosphorylated and inhibited by Akt and suppresses mTOR signalling
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The Rag GTPases Bind Raptor and Mediate Amino Acid Signaling to mTORC1
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Prolonged Rapamycin Treatment Inhibits mTORC2 Assembly and Akt/PKB
Sarbassov, D. D., Ali, S. M., Sengupta, S., Sheen, J.-H., Hsu, P. P., Bagley, A. F., Markhard, A. L., & Sabatini, D. M. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.03.029 · Cited by 2,365
Mammalian TOR complex 2 controls the actin cytoskeleton and is rapamycin insensitive
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Raptor, a Binding Partner of Target of Rapamycin (TOR), Mediates TOR Action
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Cited by
AKT/PKB Signaling: Navigating the Network
Manning, B. D., & Toker, A. (2017) · Cell · doi:10.1016/j.cell.2017.04.001 · Cited by 3,772
Self-citationThe Ras-ERK and PI3K-mTOR pathways: cross-talk and compensation
Mendoza, M. C., Er, E. E., & Blenis, J. (2011) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2011.03.006 · Cited by 1,817
mTOR signaling: At the crossroads of plasticity, memory and disease
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Regulation and function of ribosomal protein S6 kinase (S6K) within mTOR signalling networks
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“Related pathways that contribute to the regulation of AKT include: (1) mTORC1 phosphorylation/ stabilisation of GRB10 [174], which inhibits productive interaction of IRS with a key phosphotyrosine in IR [175]; (2) inhibition of mTORC2 by S6K1-mediated phosphorylation of rictor [176]; and (3) transcriptional upregulati…”
Background
Metadata
- Authors
- Dibble, C. C., Asara, J. M., & Manning, B. D.
- Venue
- Molecular and Cellular Biology
- Publisher
- Informa UK Limited
- Published
- 2009-11-01
- Volume
- 29
- Issue
- 21
- Pages
- 5657-5670
- ISSN
- 0270-7306 (ISSN-L)
- 1098-5549
- OpenAlex
- W2150595264
- Cited by
- 423
- References
- 73
- FWCI
- 14.28
- Type
- journal article
- Language
- en
- Open access
- green
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- Dibble, C. C., Asara, J. M., & Manning, B. D. (2009). Characterization of Rictor Phosphorylation Sites Reveals Direct Regulation of mTOR Complex 2 by S6K1. Molecular and Cellular Biology. https://doi.org/10.1128/mcb.00735-09
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