RPTOR
関連文献

“mTOR interacts with raptor to form a nutrient-sensitive complex that signals to the cell growth machinery”. Cell 110 (2):  163–75. (2002). doi:10.1016/S0092-8674(02)00808-5. PMID 12150925.
“The mammalian target of rapamycin (mTOR) partner, raptor, binds the mTOR substrates p70 S6 kinase and 4E-BP1 through their TOR signaling (TOS) motif”. J. Biol. Chem. 278 (18):  15461–4. (2003). doi:10.1074/jbc.C200665200. PMID 12604610.
“GbetaL, a positive regulator of the rapamycin-sensitive pathway required for the nutrient-sensitive interaction between raptor and mTOR”. Mol. Cell 11 (4):  895–904. (2003). doi:10.1016/S1097-2765(03)00114-X. PMID 12718876.
“Dissociation of raptor from mTOR is a mechanism of rapamycin-induced inhibition of mTOR function”. Genes Cells 9 (4):  359–66. (2004). doi:10.1111/j.1356-9597.2004.00727.x. PMID 15066126.
“Rictor, a novel binding partner of mTOR, defines a rapamycin-insensitive and raptor-independent pathway that regulates the cytoskeleton”. Curr. Biol. 14 (14):  1296–302. (2004). doi:10.1016/j.cub.2004.06.054. PMID 15268862.
“Large-scale characterization of HeLa cell nuclear phosphoproteins”. Proc. Natl. Acad. Sci. U.S.A. 101 (33):  12130–5. (2004). Bibcode: 2004PNAS..10112130B. doi:10.1073/pnas.0404720101. PMC 514446. PMID 15302935. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC514446/.
“Mammalian TOR complex 2 controls the actin cytoskeleton and is rapamycin insensitive”. Nat. Cell Biol. 6 (11):  1122–8. (2004). doi:10.1038/ncb1183. PMID 15467718.
“Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex”. Science 307 (5712):  1098–101. (2005). Bibcode: 2005Sci...307.1098S. doi:10.1126/science.1106148. PMID 15718470.
“Rheb binds and regulates the mTOR kinase”. Curr. Biol. 15 (8):  702–13. (2005). doi:10.1016/j.cub.2005.02.053. PMID 15854902.
“Redox regulation of the nutrient-sensitive raptor-mTOR pathway and complex”. J. Biol. Chem. 280 (47):  39505–9. (2005). doi:10.1074/jbc.M506096200. PMID 16183647.
“Nutrients suppress phosphatidylinositol 3-kinase/Akt signaling via raptor-dependent mTOR-mediated insulin receptor substrate 1 phosphorylation”. Mol. Cell. Biol. 26 (1):  63–76. (2006). doi:10.1128/MCB.26.1.63-76.2006. PMC 1317643. PMID 16354680. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1317643/.
“Turnover of the active fraction of IRS1 involves raptor-mTOR- and S6K1-dependent serine phosphorylation in cell culture models of tuberous sclerosis”. Mol. Cell. Biol. 26 (17):  6425–34. (2006). doi:10.1128/MCB.01254-05. PMC 1592824. PMID 16914728. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1592824/.
“Human cytomegalovirus infection alters the substrate specificities and rapamycin sensitivities of raptor- and rictor-containing complexes”. Proc. Natl. Acad. Sci. U.S.A. 103 (38):  14182–7. (2006). Bibcode: 2006PNAS..10314182K. doi:10.1073/pnas.0605825103. PMC 1599931. PMID 16959881. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1599931/.
“A probability-based approach for high-throughput protein phosphorylation analysis and site localization”. Nat. Biotechnol. 24 (10):  1285–92. (2006). doi:10.1038/nbt1240. PMID 16964243.
“Global, in vivo, and site-specific phosphorylation dynamics in signaling networks”. Cell 127 (3):  635–48. (2006). doi:10.1016/j.cell.2006.09.026. PMID 17081983.