Phosphorylation and Regulation of Akt/PKB by the Rictor-mTOR Complex
By Dos D. Sarbassov, D. Guertin, Siraj M. Ali, David M. Sabatini. Science, 2005
5,749 citations recorded by the source corpus.
Subfields: Molecular Biology
View Paper: https://www.semanticscholar.org/paper/719d66e16db86cdadcdefb101144d1861e3cb0e3
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In Molecular Biology
- David M. Sabatini
- M. Laplante
- Michael N. Hall
- K. Guan
- R. A. Saxton
- Lewis C. Cantley
- L. Bar-Peled
- T. Franke
Citations in the corpus
- PI3K/Akt: getting it right matters (2008, background): “mTORC2 directly phosphorylates the HM site in vitro and enhances subsequent phosphorylation of Akt by PDK1 (Sarbassov et al., 2005).”
- PRAS40 is an insulin-regulated inhibitor of the mTORC1 protein kinase. (2007, methodology): “shRNA-encoding plasmids were co-transfected with the Delta VPR envelope and CMV VSV-G packaging plasmids into actively growing HEK-293T using FuGENE 6 transfection reagent as previously described (Ali and Sabatini, 2005; Sarbassov et al., 2005).”
- ROS and ROS-Mediated Cellular Signaling (2016, background): “Afterwards, the activated PI3K catalyzes the synthesis of phosphatidylinositol 3,4,5-triphosphate (PIP3), from phosphatidylinositol 4,5-bisphosphate (PIP2) [88].”
- Defining the role of mTOR in cancer. (2007, background): “…10 years, scientists used rapamycin to uncover mTOR-dependent processes showing that mTOR regulates cell growth by controlling mRNA translation, ribosome biogenesis, autophagy, and metabolism (Figure 1A) (reviewed in Guertin and Sabatini, 2005; Sarbassov et al., 2005a; Wullschleger et al., 2006).”
- PHLPP and a second isoform, PHLPP2, differentially attenuate the amplitude of Akt signaling by regulating distinct Akt isoforms. (2007, background): “Phosphorylation of this second site is regulated by the TORC-2 protein complex (SIN1-mLST8-rictor-mTOR) (Jacinto et al., 2006; Sarbassov et al., 2005), although whether via direct phosphorylation or indirectly, for example by modulating the stability of the phosphate at this site, remains to be esta”
- The Molecular Bases of Training Adaptation (2007, background): “added to existing myofibres or combine and form new contractile filaments, each providing additional contractile machinery with which to generate force (Bolster et al. 2003a; Rennie et al. 2004; Sartorelli and Fulco 2004).”
- Leveraging molecular structure and bioactivity with chemical language models for de novo drug design (2023, background): “In response to growth factor receptor and PI3K activation, AKT is phosphorylated on Ser473 by the Rictor-mTOR complex 62 .”
- Phosphatidylinositol 5-phosphate 4-kinase (PIP4K) regulates TOR signaling and cell growth during Drosophila development (2013, background): “We also studied the phosphorylation of protein kinase B (AKT) at S505 (p-AKT, equivalent to S473 in mammalian AKT) by the rapamycin-insensitive TORC2 complex (26).”