GbetaL, a positive regulator of the rapamycin-sensitive pathway required for the nutrient-sensitive interaction between raptor and mTOR.
By Do Hyung Kim, Dos D. Sarbassov, Siraj M. Ali, R. Latek, Kalyani V. P. Guntur, H. Erdjument‐Bromage, Paul Tempst, David M. Sabatini. Molecules and Cells, 2003
1,012 citations recorded by the source corpus.
Subfields: Molecular Biology
View Paper: https://www.semanticscholar.org/paper/a3054a1ef29c20edfac240b9d646448fd790f375
How researchers see this paper
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In Molecular Biology
- David M. Sabatini
- M. Laplante
- Michael N. Hall
- R. A. Saxton
- R. Loewith
- Nahum Sonenberg
- D. Guertin
- Timothy R. Peterson
Citations in the corpus
- Growing roles for the mTOR pathway. (2005, background): “This is a bit odd because FKBP12–rapamycin binds to a region adjacent to GbL and the mTOR kinase domain but >1000 amino acids away from where raptor binds to mTOR [7,8].”
- Akt-dependent regulation of NF-{kappa}B is controlled by mTOR and Raptor in association with IKK. (2008, background): “TORC1 is comprised of mTOR, Raptor, and G L (Hara et al. 2002; Kim et al. 2002, 2003), while TORC2 is comprised of mTOR, Rictor, and G L (Sarbassov et al. 2005).”
- mTOR Signaling in Growth, Metabolism, and Disease. (2017, background): “1B, Kim et al. 2002; Hara et al. 2002; Kim et al. 2003).”
- Defining the role of mTOR in cancer. (2007, background): “…for oncology. mTORC1 Signaling in Cancer Besides mTOR, mTORC1 contains RAPTOR (regulatory associated protein of mTOR), mLST8 (also known as GβL), and PRAS40 (proline-rich AKT substrate 40 kDa) (Haar et al., 2007; Hara et al., 2002; Kim et al., 2002, 2003; Loewith et al., 2002; Sancak et al., 2007).”
- mTOR Signaling in Growth, Metabolism, and Disease (2017, background): “…known as mTOR Complex 1 (mTORC1) and 2 (mTORC2) (Figure 1A). mTORC1 is defined by its three core components: mTOR, Raptor (regulatory protein associated with mTOR), and mLST8 (mammalian lethal with Sec13 protein 8, also known as GßL) (Figure 1B; Kim et al., 2002, 2003; Hara et al., 2002).”
- mTOR, translation initiation and cancer (2006, background): “…et al., 2005; Stephens et al., 2005; Petroulakis et al., 2006) (Figure 2). mTOR promotes the phosphorylation and activation of S6K and the hierarchial phosphorylation the 4E-BPs (Gingras et al., 2001; Jacinto and Hall, 2003; Kim et al., 2003; Ruggero and Pandolfi, 2003; Kim and Sabatini, 2004).”
- SIN1/MIP1 maintains rictor-mTOR complex integrity and regulates Akt phosphorylation and substrate specificity. (2006, background): “Mammalian TOR complex 1 (TORC1) is rapamycin-sensitive and consists of mTOR, raptor, and mLST8 (GbL), which are the orthologs of yeast TOR1/2, KOG1, and LST8, respectively (Hara et al., 2002; Kim et al., 2002, 2003; Loewith et al., 2002).”
- Mammalian TOR complex 2 controls the actin cytoskeleton and is rapamycin insensitive (2004, background): “Like TOR, LST8 and KOG1 have obvious sequence homologues in all eukaryotic genomes examined, and mammalian TOR (mTOR) forms a rapamycin-sensitive, TORC1-like complex with mLST8 (GβL) and raptor (mKOG1”
- Regulation of the mTOR complex 1 pathway by nutrients, growth factors, and stress (2010, background): “Despite being a core component of mTORC1 (Kim et al., 2003; Loewith et al., 2002), the role of mLST8 remains unclear, because its deletion has no effect on mTORC1 activity in vivo or in vitro (Guertin et al., 2006).”
- Targets of curcumin (2011, background): “mTOR also functions as a central sensor of cellular nutrient/amino acid levels [104,111,112], cellular energy status [111], cellular redox status [113], and mitogen stimulation, particularly from insulin, IGF-1, and IGF-2 [114,115].”