ArticleOncogene2012
Integrity of mTORC2 is dependent on the rictor Gly-934 site.
Article in Oncogene, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 22 citations in OpenAlex.
- RICTOR regulates an interspecies crosstalk that influences longevity through a novel methionine cycle-mitophagy axis.bioRxiv : the preprint server for biology · 2025Article
- mTORC2 disruption reprograms nutrient-driven behavioral adaptations inmicroPublication biology · 2025Article
- Unmasking the tumourigenic role of SIN1/MAPKAP1 in the mTOR complex 2.Clinical and translational medicine · 2023Review
- UBXN2A suppresses the Rictor-mTORC2 signaling pathway, an established tumorigenic pathway in human colorectal cancer.Oncogene · 2023Article
- Concomitant targeting of the mTOR/MAPK pathways: novel therapeutic strategy in subsets ofOncotarget · 2018Article
- Central Regulatory Role for SIN1 in Interferon γ (IFNγ) Signaling and Generation of Biological Responses.The Journal of biological chemistry · 2017Article
- The TOR Signaling Pathway in Spatial and Temporal Control of Cell Size and Growth.Frontiers in cell and developmental biology · 2017Review
- Macrophage IKKα Deficiency Suppresses Akt Phosphorylation, Reduces Cell Survival, and Decreases Early Atherosclerosis.Arteriosclerosis, thrombosis, and vascular biology · 2016Article
- Interferon γ (IFNγ) Signaling via Mechanistic Target of Rapamycin Complex 2 (mTORC2) and Regulatory Effects in the Generation of Type II Interferon Biological Responses.The Journal of biological chemistry · 2016Article
- β-hydroxyisovaleryl-shikonin induces human cervical cancer cell apoptosis via PI3K/AKT/mTOR signaling.Oncology letters · 2015Article
- Point mutations of the mTOR-RHEB pathway in renal cell carcinoma.Oncotarget · 2015Article
- Target of Rapamycin Complex 2 regulates cell growth via Myc in Drosophila.Scientific reports · 2015Article
- Rictor negatively regulates high-affinity receptors for IgE-induced mast cell degranulation.Journal of immunology (Baltimore, Md. : 1950) · 2014Article
- Autoregulation of the mechanistic target of rapamycin (mTOR) complex 2 integrity is controlled by an ATP-dependent mechanism.The Journal of biological chemistry · 2013Article
- The evolution of the TOR pathway and its role in cancer.Oncogene · 2013Review
- Rictor regulates cell migration by suppressing RhoGDI2.Oncogene · 2013Article
- Shedding new light on neurodegenerative diseases through the mammalian target of rapamycin.Progress in neurobiology · 2012Review
- Regulatory effects of mTORC2 complexes in type I IFN signaling and in the generation of IFN responses.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
Corrections and comments
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Authors and funding
7 authors at 4 institutions in 2 countries.
Funding
Abstract
Growth factor signaling coupled to activation of the phosphatidylinositol-3-OH kinase (PI3K)/Akt pathway plays a crucial role in the regulation of cell proliferation and survival. The key regulatory kinase of Akt has been identified as mammalian target of rapamycin complex 2 (mTORC2), which functions as the PI3K-dependent Ser-473 kinase of Akt. This kinase complex is assembled by mTOR and its essential components rictor, Sin1 and mLST8. The recent genetic screening study in Caenorhabditis elegans has linked a specific point mutation of rictor to an elevated storage of fatty acids that resembles the rictor deficiency phenotype. In our study, we show that in mammalian cells the analogous single rictor point mutation (G934E) prevents the binding of rictor to Sin1 and the assembly of mTORC2, but this mutation does not interfere with the binding of the rictor-interacting protein Protor. A substitution of the rictor Gly-934 residue to a charged amino acid prevents formation of the rictor/Sin1 heterodimer. The cells expressing the rictor G934E mutant remain deficient in the mTORC2 signaling, as detected by the reduced phosphorylation of Akt on Ser-473 and a low cell proliferation rate. Thus, although a full length of rictor is required to interact with its binding partner Sin1, a single amino acid of rictor Gly-934 controls its interaction with Sin1 and assembly of mTORC2.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.