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The DOI matches its Crossref record; 8 of the 8 references it cites were found in a registry or an index.

Dihydroxyacetone phosphate signals glucose availability to mTORC1

Orozco, Jose M., Krawczyk, Patrycja A., Scaria, Sonia M., Cangelosi, Andrew L., Chan, Sze Ham, Kunchok, Tenzin, Lewis, Caroline A., Sabatini, David M.·2020·Nature Metabolism
DOI 10.1038/s42255-020-0250-5PMC PMC7995735

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Crossref · 10.1038/s42255-020-0250-5

Cites

8 of 8 references verified0 citation errors · 0 not checkable

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  • mTORC1 is regulated by nutrients and hormonal cues, notably amino acids, glucose, oxygen, and cholesterol.

    “mTORC1 is regulated by a wide range of nutrients and hormonal cues, most notably the availability of amino acids, but also glucose, oxygen, and cholesterol 1–3.”

    From Targeting the biology of aging with mTOR inhibitors (2023) · cites this paper as [2]

    The Abstract and the Results section on GATOR-Rag signaling say that amino acids and glucose regulate mTORC1. The passages found do not establish regulation by hormonal cues, oxygen, or cholesterol, so this source supports only part of the cited sentence. (LLM, conf=0.86)

    Experimental — accuracy not yet measured

  • The glycolytic intermediate dihydroxyacetone phosphate is sensed via a GATOR-dependent mechanism.

    “Finally, while glucose is not directly sensed by mTORC1, the glycolytic intermediate dihydroxyacetone phosphate (DHAP) is sensed via a GATOR-dependent mechanism 2.”

    From Targeting the biology of aging with mTOR inhibitors (2023) · cites this paper as [2]

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Citations

Cites

Flagged first, then by citations

Research works printed but not linked: 33

  1. Kubrusly, M. S. et al. A role for mammalian target of rapamycin (mTOR) pathway in non-alcoholic steatohepatitis-related cirrhosis. Histol. Histopathol. 25, 1123–1131 (2010).
  2. Guillén, C. & Benito, M. mTORC1 overactivation as a key aging factor in the progression to type 2 diabetes mellitus. Front. Endocrinol. 9, 621 (2018). · DOI
  3. Ardestani, A., Lupse, B., Kido, Y., Leibowitz, G. & Maedler, K. mTORC1 signaling: a double-edged sword in diabetic β cells. Cell Metab. 27, 314–331 (2018). · DOI
  4. Lee, P. L., Tang, Y., Li, H. & Guertin, D. A. Raptor/mTORC1 loss in adipocytes causes progressive lipodystrophy and fatty liver disease. Mol. Metab. 5, 422–432 (2016). · DOI
  5. Inoki, K., Zhu, T. & Guan, K.-L. TSC2 mediates cellular energy response to control cell growth and survival. Cell 115, 577–590 (2003). · DOI · Paper page
  6. Shaw, R. J. et al. The LKB1 tumor suppressor negatively regulates mTOR signaling. Cancer Cell 6, 91–99 (2004). · DOI
  7. Gwinn, D. M. & Shaw, R. J. AMPK control of mTOR signaling and growth. in The Enzymes Vol. 28 (eds Tamanoi, F. & Hall, M. N.) 49–75 (Academic Press, 2010). · DOI
  8. Efeyan, A. et al. Regulation of mTORC1 by the Rag GTPases is necessary for neonatal autophagy and survival. Nature 493, 679–683 (2013). · DOI
  9. Wolfson, R. L. et al. KICSTOR recruits GATOR1 to the lysosome and is necessary for nutrients to regulate mTORC1. Nature 543, 438–442 (2017). · DOI
  10. Kalender, A. et al. Metformin, independent of AMPK, inhibits mTORC1 in a Rag GTPase-dependent manner. Cell Metab. 11, 390–401 (2010). · DOI · Paper page
  11. Buller, C. L., Heilig, C. W. & Brosius, F. C. GLUT1 enhances mTOR activity independently of TSC2 and AMPK. Am. J. Physiol. Renal Physiol. 301, F588–F596 (2011). · DOI
  12. Almacellas, E. et al. Phosphofructokinases axis controls glucose-dependent mTORC1 activation driven by E2F1. iScience 20, 434–448 (2019). · DOI
  13. Roberts, D. J., Tan-Sah, V. P., Ding, E. Y., Smith, J. M. & Miyamoto, S. Hexokinase-II positively regulates glucose starvation induced autophagy through TORC1 inhibition. Mol. Cell 53, 521–533 (2014). · DOI
  14. Zhang, C.-S. et al. Fructose-1,6-bisphosphate and aldolase mediate glucose sensing by AMPK. Nature 548, 112–116 (2017). · DOI
  15. Lee, M. N. et al. Glycolytic flux signals to mTOR through glyceraldehyde-3-phosphate dehydrogenase-mediated regulation of Rheb. Mol. Cell. Biol. 29, 3991–4001 (2009). · DOI
  16. Sharma, S., Guthrie, P. H., Chan, S. S., Haq, S. & Taegtmeyer, H. Glucose phosphorylation is required for insulin-dependent mTOR signalling in the heart. Cardiovasc. Res. 76, 71–80 (2007). · DOI
  17. Karlstaedt, A., Khanna, R., Thangam, M. & Taegtmeyer, H. Glucose 6-phosphate accumulates via phosphoglucose isomerase inhibition in heart muscle. Circ. Res. 126, 60–74 (2020). · DOI
  18. Shiraj, S. et al. Glucose regulation of load‐induced mTOR signaling and ER stress in mammalian heart. J. Am. Heart Assoc. 2, e004796 (2013). · DOI
  19. Kanehisa, M. & Goto, S. KEGG: Kyoto Encyclopedia of Genes and Genomes. Nucleic Acids Res. 28, 27–30 (2000). · DOI · Paper page
  20. Sakai, K., Hasumi, K. & Endo, A. Two glyceraldehyde-3-phosphate dehydrogenase isozymes from the koningic acid producer Trichoderma koningii. Eur. J. Biochem. 193, 195–202 (1990). · DOI
  21. Liberti, M. V. et al. A predictive model for selective targeting of the warburg effect through GAPDH inhibition with a natural product. Cell Metab. 26, 648–659 (2017). · DOI
  22. Rieder, S. V. & Rose, I. A. The mechanism of the triosephosphate isomerase reaction. J. Biol. Chem. 234, 1007–1010 (1959). · DOI
  23. Menon, D. et al. Lipid sensing by mTOR complexes via de novo synthesis of phosphatidic acid. J. Biol. Chem. 292, 6303–6311 (2017). · DOI
  24. Ye, J. et al. GCN2 sustains mTORC1 suppression upon amino acid deprivation by inducing Sestrin2. Genes Dev. 29, 2331–2336 (2015). · DOI
  25. Düvel, K. et al. Activation of a metabolic gene regulatory network downstream of mTOR complex 1. Mol. Cell 39, 171–183 (2010). · DOI · Paper page
  26. Peterson, T. R. et al. mTOR complex 1 regulates lipin 1 localization to control the SREBP pathway. Cell 146, 408–420 (2011). · DOI
  27. Herman, M. A., She, P., Peroni, O. D., Lynch, C. J. & Kahn, B. B. Adipose tissue branched chain amino acid metabolism (BCAA) modulates circulating BCAA levels. J. Biol. Chem. 285, 11348–11356 (2010). · DOI
  28. Jang, C. et al. The small intestine converts dietary fructose into glucose and organic acids. Cell Metab. 27, 351–361 (2018). · DOI · Paper page
  29. Herman, M. A. & Samuel, V. T. The sweet path to metabolic demise: fructose and lipid synthesis. Trends Endocrinol. Metab. 27, 719–730 (2016). · DOI
  30. Frias, M. A. et al. Phosphatidic acid drives mTORC1 lysosomal translocation in the absence of amino acids. J. Biol. Chem. 295, 263–274 (2020). · DOI
  31. Dennis, P. B. et al. Mammalian TOR: a homeostatic ATP sensor. Science 294, 1102–1105 (2001). · DOI · Paper page
  32. Yang, W.-C. et al. Simultaneous quantification of metabolites involved in central carbon and energy metabolism using reversed-phase liquid chromatography−mass spectrometry and in vitro 13C labeling. Anal. Chem. 80, 9508–9516 (2008). · DOI
  33. Jannasch, A., Sedlak, M. & Adamec, J. Quantification of pentose phosphate pathway (PPP) metabolites by LC–MS. in Metabolic Profiling: Methods and Protocols (ed. Metz, T. O.) 159–171 (Humana Press, 2011). · DOI

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Metadata

Authors
Orozco, J. M., Krawczyk, P. A., Scaria, S. M., Cangelosi, A. L., Chan, S. H., Kunchok, T., Lewis, C. A., & Sabatini, D. M.
ORCID
Venue
Nature Metabolism
Publisher
Springer Science and Business Media LLC
Published
2020-07-27
Volume
2
Issue
9
Pages
893-901
ISSN
2522-5812
DOI
10.1038/s42255-020-0250-5
PMC
PMC7995735
Cited by
242
References
8
Language
en
Licence
Funders
  • U.S. Department of Health & Human Services | NIH | National Cancer Institute (F30CA210373, R01 CA129105)
  • U.S. Department of Health & Human Services | NIH | National Institute of General Medical Sciences (T32GM007753)
  • U.S. Department of Health & Human Services | NIH | National Institute of Diabetes and Digestive and Kidney Diseases (F31DK113665)
  • Howard Hughes Medical Institute
  • American Cancer Society

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