mTOR interacts with raptor to form a nutrient-sensitive complex that signals to the cell growth machinery.

By Do Hyung Kim, Dos D. Sarbassov, Siraj M. Ali, J. E. King, R. Latek, H. Erdjument‐Bromage, Paul Tempst, David M. Sabatini. Cell, 2002

3,106 citations recorded by the source corpus.

Subfields: Molecular Biology

View Paper: https://www.semanticscholar.org/paper/13d1dfda36de9166c8565c9a1cf542a75d853c44

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Citations in the corpus

Lysosomal metabolomics reveals V-ATPase- and mTOR-dependent regulation of amino acid efflux from lysosomes (2017, background): “3B) (16, 17), we asked if mTORC1 regulates the abundance of amino acids in lysosomes.”
mTOR Controls Cell Cycle Progression through Its Cell Growth Effectors S6K1 and 4E-BP1/Eukaryotic Translation Initiation Factor 4E (2004, background): “A recently identified mTOR-interacting protein, raptor, links mTOR to substrates such as 4E-BP1 (16, 25) by binding to the TOR signaling (TOS) motif in the C terminus of 4E-BP1 (either directly or indirectly), enabling mTOR-dependent phosphorylation of 4E-BP1 in response to nutrients or growth facto”
GbetaL, a positive regulator of the rapamycin-sensitive pathway required for the nutrient-sensitive interaction between raptor and mTOR. (2003, methodology): “Because FKBP12-rapamycin binds directly N-ter- levels (Kim et al., 2002).”
Regulation of the mTOR complex 1 pathway by nutrients, growth factors, and stress (2010, background): “Raptor has many functions, and it regulates mTORC1 assembly and recruits kinase substrates, such as 4E-BP1 (Hara et al., 2002; Kim et al., 2002).”
Metabolic competition in the tumor microenvironment is a driver of cancer progression (2015, background): “We wondered whether higher glycolysis in P tumors limited glucose in the microenvironment and contributed to TIL hyporesponsiveness. mTOR is an environmental sensor, and mTOR pathway signals decrease when nutrients are restricted (Gatenby and Gillies, 2004; Kim et al., 2002).”
Defining the role of mTOR in cancer. (2007, background): “Nearly a decade after the discovery of mTOR, researchers found that mTOR nucleates a rapamycinand nutrient-sensitive multiprotein complex (now called mTORC1) (Hara et al., 2002; Kim et al., 2002; Loewith et al., 2002).”
mTORC1 controls mitochondrial activity and biogenesis through 4E-BP-dependent translational regulation. (2013, background): “mTOR forms two distinct complexes, mTOR complex 1 (mTORC1) and 2 (mTORC2), which differ in their composition, downstream targets, regulation, and sensitivity to the allosteric inhibitor rapamycin (Hara et al., 2002; Kim et al., 2002; Sarbassov et al., 2004).”
Active-Site Inhibitors of mTOR Target Rapamycin-Resistant Outputs of mTORC1 and mTORC2 (2009, background): “mTOR exists in two complexes, mTORC1 [ 1 ,2] and mTORC2 [3,4], which are differentially regulated, have distinct substrate specificities, and are differentially sensitive to rapamycin.”
mTOR Signaling in Growth, Metabolism, and Disease. (2017, positive): “1B, Kim et al. 2002; Hara et al. 2002; Kim et al. 2003).”
Target of Rapamycin (TOR) in Nutrient Signaling and Growth Control (2011, result): “…of TORCs in other eukaryotes, including plants, worms, flies, and mammals (Table 1), showed that the two complexes, like TOR itself, are conserved and gave further support to the above model (Hara et al. 2002; Kim et al. 2002; Loewith et al. 2002; Jacinto et al. 2004; Sarbassov et al. 2004).”
A nutrient sensor mechanism controls Drosophila growth. (2003, background): “cells and in yeast (Hara et al., 2002; Kim et al., 2002;1Institute for Signaling Loewith et al., 2002).”