References
Pochini, L., Scalise, M., Galluccio, M. & Indiveri, C. Membrane transporters for the special amino acid glutamine: structure/function relationships and relevance to human health. Front. Chem. 2, 61 (2014).
Jin, L., Alesi, G.N. & Kang, S. Glutaminolysis as a target for cancer therapy. Oncogene 35, 3619–3625 (2016).
Hassanein, M. et al. SLC1A5 mediates glutamine transport required for lung cancer cell growth and survival. Clin. Cancer Res. 19, 560–570 (2013).
van Geldermalsen, M. et al. ASCT2/SLC1A5 controls glutamine uptake and tumour growth in triple-negative basal-like breast cancer. Oncogene 35, 3201–3208 (2016).
Schulte, M.L. et al. Non-invasive glutamine PET reflects pharmacological inhibition of BRAFV600Ein vivo. Mol. Imaging Biol. 19, 421–428 (2017).
Gao, P. et al. c-Myc suppression of miR-23a/b enhances mitochondrial glutaminase expression and glutamine metabolism. Nature 458, 762–765 (2009).
Watanabe, T. et al. Differential gene expression signatures between colorectal cancers with and without KRAS mutations: crosstalk between the KRAS pathway and other signalling pathways. Eur. J. Cancer 47, 1946–1954 (2011).
Romero, R. et al. Keap1 loss promotes Kras-driven lung cancer and results in dependence on glutaminolysis. Nat. Med. 23, 1362–1368 (2017).
Shukla, K. et al. Design, synthesis, and pharmacological evaluation of bis-2-(5-henylacetamido-1,2,4-thiadiazol-2-yl)ethyl sulfide 3 (BPTES) analogs as glutaminase inhibitors. J. Med. Chem. 55, 10551–10563 (2012).
Harding, J.J. et al. Safety and tolerability of increasing doses of CB-839, a first-in-class, orally administered small molecule inhibitor of glutaminase, in solid tumors. J. Clin. Oncol. 33, 2512 (2015).
Rhoads, J.M. et al. Glutamine metabolism stimulates intestinal cell MAPKs by a cAMP-inhibitable, Raf-independent mechanism. Gastroenterology 118, 90–100 (2000).
Willems, L. et al. Inhibiting glutamine uptake represents an attractive new strategy for treating acute myeloid leukemia. Blood 122, 3521–3532 (2013).
Schulte, M.L., Khodadadi, A.B., Cuthbertson, M.L., Smith, J.A. & Manning, H.C. 2-Amino-4-bis(aryloxybenzyl)aminobutanoic acids: a novel scaffold for inhibition of ASCT2-mediated glutamine transport. Bioorg. Med. Chem. Lett. 26, 1044–1047 (2016).
Esslinger, C.S., Cybulski, K.A. & Rhoderick, J.F. Nγ-Aryl glutamine analogues as probes of the ASCT2 neutral amino acid transporter binding site. Bioorg. Med. Chem. 13, 1111–1118 (2005).
Lomenick, B. et al. Target identification using drug affinity responsive target stability (DARTS). Proc. Natl. Acad. Sci. USA 106, 21984–21989 (2009).
Canul-Tec, J.C. et al. Structure and allosteric inhibition of excitatory amino acid transporter 1. Nature 544, 446–451 (2017).
Fuchs, B.C. & Bode, B.P. Amino acid transporters ASCT2 and LAT1 in cancer: partners in crime? Semin. Cancer Biol. 15, 254–266 (2005).
Nicklin, P. et al. Bidirectional transport of amino acids regulates mTOR and autophagy. Cell 136, 521–534 (2009).
Vichai, V. & Kirtikara, K. Sulforhodamine B colorimetric assay for cytotoxicity screening. Nat. Protoc. 1, 1112–1116 (2006).
Rathmell, J.C. T cell Myc-tabolism. Immunity 35, 845–846 (2011).
Skala, M. & Ramanujam, N. Multiphoton redox ratio imaging for metabolic monitoring in vivo. Methods Mol. Biol. 594, 155–162 (2010).
Walsh, A.J. et al. Quantitative optical imaging of primary tumor organoid metabolism predicts drug response in breast cancer. Cancer Res. 74, 5184–5194 (2014).
DeBerardinis, R.J., Sayed, N., Ditsworth, D. & Thompson, C.B. Brick by brick: metabolism and tumor cell growth. Curr. Opin. Genet. Dev. 18, 54–61 (2008).
Hanover, J.A., Krause, M.W. & Love, D.C. The hexosamine signaling pathway: O-GlcNAc cycling in feast or famine. Biochim. Biophys. Acta 1800, 80–95 (2010).
Obeid, L.M., Linardic, C.M., Karolak, L.A. & Hannun, Y.A. Programmed cell death induced by ceramide. Science 259, 1769–1771 (1993).
Tresse, E., Kosta, A., Giusti, C., Luciani, M.F. & Golstein, P. A UDP-glucose derivative is required for vacuolar autophagic cell death. Autophagy 4, 680–691 (2008).
Sentelle, R.D. et al. Ceramide targets autophagosomes to mitochondria and induces lethal mitophagy. Nat. Chem. Biol. 8, 831–838 (2012).
Dall'Armi, C., Devereaux, K.A. & Di Paolo, G. The role of lipids in the control of autophagy. Curr. Biol. 23, R33–R45 (2013).
Shatz, O., Holland, P., Elazar, Z. & Simonsen, A. Complex relations between phospholipids, autophagy, and neutral lipids. Trends Biochem. Sci. 41, 907–923 (2016).
Huang, F., Zhang, Q., Ma, H., Lv, Q. & Zhang, T. Expression of glutaminase is upregulated in colorectal cancer and of clinical significance. Int. J. Clin. Exp. Pathol. 7, 1093–1100 (2014).
Xiang, Y. et al. Targeted inhibition of tumor-specific glutaminase diminishes cell-autonomous tumorigenesis. J. Clin. Invest. 125, 2293–2306 (2015).
Seltzer, M.J. et al. Inhibition of glutaminase preferentially slows growth of glioma cells with mutant IDH1. Cancer Res. 70, 8981–8987 (2010).
Gross, M.I. et al. Antitumor activity of the glutaminase inhibitor CB-839 in triple-negative breast cancer. Mol. Cancer Ther. 13, 890–901 (2014).
Suzuki, S. et al. Phosphate-activated glutaminase (GLS2), a p53-inducible regulator of glutamine metabolism and reactive oxygen species. Proc. Natl. Acad. Sci. USA 107, 7461–7466 (2010).
Chiu, M. et al. GPNA inhibits the sodium-independent transport system L for neutral amino acids. Amino Acids 49, 1365–1372 (2017).
McKinley, E.T., Zhao, P., Coffey, R.J., Washington, M.K. & Manning, H.C. 3′-Deoxy-3′-[18F]-fluorothymidine PET imaging reflects PI3K–mTOR-mediated pro-survival response to targeted therapy in colorectal cancer. PLoS One 9, e108193 (2014).
Wiza, C., Nascimento, E.B. & Ouwens, D.M. Role of PRAS40 in Akt and mTOR signaling in health and disease. Am. J. Physiol. Endocrinol. Metab. 302, E1453–E1460 (2012).
Santio, N.M. et al. The PIM1 kinase promotes prostate cancer cell migration and adhesion via multiple signalling pathways. Exp. Cell Res. 342, 113–124 (2016).
Rhoads, J.M. et al. L-Glutamine stimulates intestinal cell proliferation and activates mitogen-activated protein kinases. Am. J. Physiol. 272, G943–G953 (1997).
CAS PubMed Google Scholar
Meiler, J. & Baker, D. ROSETTALIGAND: protein–small molecule docking with full side-chain flexibility. Proteins 65, 538–548 (2006).
Kondo, J. et al. Retaining cell–cell contact enables preparation and culture of spheroids composed of pure primary cancer cells from colorectal cancer. Proc. Natl. Acad. Sci. USA 108, 6235–6240 (2011).
McKinley, E.T. et al. 18FDG-PET predicts pharmacodynamic response to OSI-906, a dual IGF-1R/IR inhibitor, in preclinical mouse models of lung cancer. Clin. Cancer Res. 17, 3332–3340 (2011).