CoChat
Sign Up
Cited by 308

The DOI matches its Crossref record; 10 of the 10 references it cites were found in a registry or an index.

Mechanism of arginine sensing by CASTOR1 upstream of mTORC1

Saxton, Robert A., Chantranupong, Lynne, Knockenhauer, Kevin E., Schwartz, Thomas U., Sabatini, David M.·2016·Nature
DOI 10.1038/nature19079PMC PMC4988899
Open this paper in CoChat — free account

Overview

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1038/nature19079

Cites

10 of 10 references verified0 citation errors · 0 not checkable

Statistics

Verification

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

  • When arginine levels are high, CASTOR proteins bind arginine and release GATOR2, allowing recruitment of mTORC1 to the lysosome.

    “The CASTOR proteins function similarly; when arginine levels are low, the CASTOR proteins bind to and inhibit GATOR2. When arginine levels are high, CASTOR proteins bind to arginine and release GATOR2, which allows the recruitment of mTORC1 to the lysosome170,171.”

    From Targeting the biology of aging with mTOR inhibitors (2023) · cites this paper as [170]

    The paper’s Abstract and CASTOR1–GATOR2 mechanism passage say that arginine binding causes CASTOR1 to dissociate from GATOR2, followed by mTORC1 activation. But the CASTOR2 passage says CASTOR2 does not bind arginine, so the claim is too broad in saying “CASTOR proteins.” The passages also do not establish the stated recruitment of mTORC1 to the lysosome. (LLM, conf=0.88)

    Experimental — accuracy not yet measured

  • CASTOR proteins bind to and inhibit GATOR2 when arginine levels are low.

    “The CASTOR proteins function similarly; when arginine levels are low, the CASTOR proteins bind to and inhibit GATOR2. When arginine levels are high, CASTOR proteins bind to arginine and release GATOR2, which allows the recruitment of mTORC1 to the lysosome170,171.”

    From Targeting the biology of aging with mTOR inhibitors (2023) · cites this paper as [170]

    The paper’s Abstract states that CASTOR1 interacts with GATOR2 in an arginine-sensitive manner and that this interaction is required to signal arginine deprivation to mTORC1. It also describes CASTOR2 as a GATOR2 interactor, but does not establish that CASTOR2 inhibits GATOR2 when arginine is low. Thus the claim is supported for CASTOR1, not for CASTOR proteins collectively. (LLM, conf=0.78)

    Experimental — accuracy not yet measured

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Citations

Cites

Flagged first, then by citations

Research works printed but not linked: 31

  1. Laplante, M. & Sabatini, D. M. mTOR signaling in growth control and disease. Cell 149, 274–293 (2012) · DOI · Paper page
  2. Dibble, C. C. & Manning, B. D. Signal integration by mTORC1 coordinates nutrient input with biosynthetic output. Nat. Cell Biol. 15, 555–564 (2013) · DOI
  3. Ban, H. et al. Arginine and Leucine regulate p70 S6 kinase and 4E-BP1 in intestinal epithelial cells. Int. J. Mol. Med. 13, 537–543 (2004)
  4. Yao, K. et al. Dietary arginine supplementation increases mTOR signaling activity in skeletal muscle of neonatal pigs. J. Nutr. 138, 867–872 (2008) · DOI
  5. Sancak, Y. et al. The Rag GTPases bind raptor and mediate amino acid signaling to mTORC1. Science 320, 1496–1501 (2008) · DOI · Paper page
  6. Wang, S. et al. Metabolism. Lysosomal amino acid transporter SLC38A9 signals arginine sufficiency to mTORC1. Science 347, 188–194 (2015) · DOI
  7. Aravind, L. & Koonin, E. V. Gleaning non-trivial structural, functional and evolutionary information about proteins by iterative database searches. J. Mol. Biol. 287, 1023–1040 (1999) · DOI
  8. Grant, G. A. The ACT domain: a small molecule binding domain and its role as a common regulatory element. J. Biol. Chem. 281, 33825–33829 (2006) · DOI
  9. Chipman, D. M. & Shaanan, B. The ACT domain family. Curr. Opin. Struct. Biol. 11, 694–700 (2001) · DOI
  10. Chantranupong, L. et al. The Sestrins interact with GATOR2 to negatively regulate the amino-acid-sensing pathway upstream of mTORC1. Cell Reports 9, 1–8 (2014) · DOI · Paper page
  11. Parmigiani, A. et al. Sestrins inhibit mTORC1 kinase activation through the GATOR complex. Cell Reports 9, 1281–1291 (2014) · DOI · Paper page
  12. Kotaka, M., Ren, J., Lockyer, M., Hawkins, A. R. & Stammers, D. K. Structures of R- and T-state Escherichia coli aspartokinase III. Mechanisms of the allosteric transition and inhibition by lysine. J. Biol. Chem. 281, 31544–31552 (2006) · DOI
  13. Robin, A. Y. et al. A new mode of dimerization of allosteric enzymes with ACT domains revealed by the crystal structure of the aspartate kinase from Cyanobacteria. J. Mol. Biol. 399, 283–293 (2010) · DOI
  14. Dumas, R., Cobessi, D., Robin, A. Y., Ferrer, J.-L. & Curien, G. The many faces of aspartate kinases. Arch. Biochem. Biophys. 519, 186–193 (2012) · DOI
  15. Bridgham, J. T., Carroll, S. M. & Thornton, J. W. Evolution of hormone-receptor complexity by molecular exploitation. Science 312, 97–101 (2006) · DOI
  16. Coyle, S. M., Flores, J. & Lim, W. A. Exploitation of latent allostery enables the evolution of new modes of MAP kinase regulation. Cell 154, 875–887 (2013) · DOI
  17. Peisajovich, S. G., Garbarino, J. E., Wei, P. & Lim, W. A. Rapid diversification of cell signaling phenotypes by modular domain recombination. Science 328, 368–372 (2010) · DOI
  18. Andersen, K. R., Leksa, N. C. & Schwartz, T. U. Optimized E. coli expression strain LOBSTR eliminates common contaminants from His-tag purification. Proteins 81, 1857–1861 (2013) · DOI
  19. Brohawn, S. G., Leksa, N. C., Spear, E. D., Rajashankar, K. R. & Schwartz, T. U. Structural evidence for common ancestry of the nuclear pore complex and vesicle coats. Science 322, 1369–1373 (2008) · DOI
  20. Morin, A. et al. Collaboration gets the most out of software. eLife 2, e01456 (2013) · DOI
  21. Otwinowski, Z. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307–326 (1997) · DOI · Paper page
  22. Adams, P. D. et al. PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr. D Biol. Crystallogr. 66, 213–221 (2010) · DOI · Paper page
  23. Emsley, P., Lohkamp, B., Scott, W. G. & Cowtan, K. Features and development of Coot. Acta Crystallogr. D Biol. Crystallogr. 66, 486–501 (2010) · DOI · Paper page
  24. Krissinel, E. & Henrick, K. Inference of macromolecular assemblies from crystalline state. J. Mol. Biol. 372, 774–797 (2007) · DOI
  25. Gibrat, J. F., Madej, T. & Bryant, S. H. Surprising similarities in structure comparison. Curr. Opin. Struct. Biol. 6, 377–385 (1996) · DOI
  26. Waterhouse, A. M., Procter, J. B., Martin, D. M. A., Clamp, M. & Barton, G. J. Jalview Version 2—a multiple sequence alignment editor and analysis workbench. Bioinformatics 25, 1189–1191 (2009) · DOI
  27. Notredame, C., Higgins, D. G. & Heringa, J. T-Coffee: A novel method for fast and accurate multiple sequence alignment. J. Mol. Biol. 302, 205–217 (2000) · DOI
  28. Altschul, S. F., Gish, W., Miller, W., Myers, E. W. & Lipman, D. J. Basic local alignment search tool. J. Mol. Biol. 215, 403–410 (1990) · DOI · Paper page
  29. Kim, D.-H. et al. mTOR interacts with raptor to form a nutrient-sensitive complex that signals to the cell growth machinery. Cell 110, 163–175 (2002) · DOI
  30. Boussif, O. et al. A versatile vector for gene and oligonucleotide transfer into cells in culture and in vivo: polyethylenimine. Proc. Natl Acad. Sci. USA 92, 7297–7301 (1995) · DOI
  31. Tsun, Z.-Y. et al. The folliculin tumor suppressor is a GAP for the RagC/D GTPases that signal amino acid levels to mTORC1. Mol. Cell 52, 495–505 (2013) · DOI · Paper page

Cited by

Sorted by citations

Metadata

Authors
Saxton, R. A., Chantranupong, L., Knockenhauer, K. E., Schwartz, T. U., & Sabatini, D. M.
Venue
Nature
Publisher
Springer Science and Business Media LLC
Published
2016-08
Volume
536
Issue
7615
Pages
229-233
ISSN
  • 0028-0836
  • 1476-4687
DOI
10.1038/nature19079
PMC
PMC4988899
Cited by
308
References
10
Language
en
Licence
www.springer.com/tdm (tdm)

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review