ArticleBiochemical and biophysical research communications2011
Endoplasmic reticulum is a main localization site of mTORC2.
Article in Biochemical and biophysical research communications, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
44 citing papers in PubMed, 80 citations in OpenAlex.
- Rictor/mTORC2 signaling pathway protects endogenous neural stem cells to promote recovery after spinal cord injury.Neural regeneration research · 2026Article
- The spatiotemporal dynamics of MAMs: mechanisms, pathologies, and therapeutic rewiring.Cellular & molecular biology letters · 2026Review
- Structural and mechanistic basis of mTORC2 activation of protein kinase AKT/PKB.The Biochemical journal · 2026Review
- mTOR signaling and Alzheimer's disease: What we know and where we are?CNS neuroscience & therapeutics · 2024Review
- The mTORC2 signaling network: targets and cross-talks.The Biochemical journal · 2024Review
- Article
- SP1-activated USP27X-AS1 promotes hepatocellular carcinoma progression via USP7-mediated AKT stabilisation.Clinical and translational medicine · 2024Article
- Unmasking the tumourigenic role of SIN1/MAPKAP1 in the mTOR complex 2.Clinical and translational medicine · 2023Review
- Neuronal mTOR Outposts: Implications for Translation, Signaling, and Plasticity.Frontiers in cellular neuroscience · 2022Article
- Continuous variable responses and signal gating form kinetic bases for pulsatile insulin signaling and emergence of resistance.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- mTOR controls endoplasmic reticulum-Golgi apparatus trafficking of VSVg in specific cell types.Cellular & molecular biology letters · 2021Article
- Review
- TMBIM6/BI-1 contributes to cancer progression through assembly with mTORC2 and AKT activation.Nature communications · 2020Article
- mTORC2 Is Involved in the Induction of RSK Phosphorylation by Serum or Nutrient Starvation.Cells · 2020Article
- Lysosome Positioning Influences mTORC2 and AKT Signaling.Molecular cell · 2019Article
- Phosphoinositide spatially free AKT/PKB activation to all membrane compartments.Advances in biological regulation · 2019Review
- mTORC1/2 inhibitor and curcumin induce apoptosis through lysosomal membrane permeabilization-mediated autophagy.Oncogene · 2018Article
- Targeting the PI3K/Akt/mTOR signalling pathway in Cystic Fibrosis.Scientific reports · 2017Article
- The Complex Roles of Mechanistic Target of Rapamycin in Adipocytes and Beyond.Trends in endocrinology and metabolism: TEM · 2017Review
- Lipid sensing by mTOR complexes viaThe Journal of biological chemistry · 2017Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The Akt kinase is a critical effector in growth factor signaling. Activation of Akt driven by the growth factor dependent PI3K (phosphatidylinositol-3-OH kinase) is coupled to the plasma membrane translocation and phosphorylation of Akt on two sites by PDK1 (phosphoinositide-dependent protein kinase-1) on Thr-308 and by mTORC2 (mammalian Target of Rapamycin Complex 2) on Ser-473. In our study we examined the sub-cellular localization of mTORC2 and identified that this kinase complex predominantly resides on endoplasmic reticulum (ER). Our immunostaining analysis did not show a substantial co-localization of the mTORC2 component rictor with Golgi, lysosome, clathrin-coated vesicles, early endosomes, or plasma membrane but indicated a strong co-localization of rictor with ribosomal protein S6 and ER marker. Our biochemical study also identified the mTORC2 components rictor, SIN1, and mTOR as the highly abundant proteins in the ER fraction, whereas only small amount of these proteins are detected in the plasma membrane and cytosolic fractions. We found that growth factor signaling does not alter the ER localization of mTORC2 and also does not induce its translocation to the plasma membrane. Based on our study we suggest that the mTORC2-dependent phosphorylation of Akt on Ser-473 takes place on the surface of ER.
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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.