Evidence map›Paper›PMID 28416685›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2017

SNAT7 is the primary lysosomal glutamine exporter required for extracellular protein-dependent growth of cancer cells.

Quentin Verdon, Marielle Boonen, Christopher Ribes, Michel Jadot, Bruno Gasnier, Corinne Sagné

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
3.9field-weighted citation impact, top 7% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

39 citing papers in PubMed, 74 citations in OpenAlex.

  1. Review
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  10. AmSphere · 2024
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  12. Review
  13. Review
  14. Article
  15. Lysosomal solute and water transport.The Journal of cell biology · 2022
    Review
  16. Article
  17. Review
  18. SNAT7 regulates mTORC1 via macropinocytosis.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  19. Review
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 2 countries.

Quentin VerdonNeurophotonics Laboratory, Paris Descartes University, CNRS UMR 8250, Sorbonne Paris Cité, F-75006 Paris, France.
Marielle BoonenUnité de Recherche en Physiologie Moléculaire (URPhyM), Laboratoire de Chimie Physiologique, Narilis, University of Namur, 5000 Namur, Belgium.
Christopher RibesNeurophotonics Laboratory, Paris Descartes University, CNRS UMR 8250, Sorbonne Paris Cité, F-75006 Paris, France.
Michel JadotUnité de Recherche en Physiologie Moléculaire (URPhyM), Laboratoire de Chimie Physiologique, Narilis, University of Namur, 5000 Namur, Belgium.
Bruno GasnierNeurophotonics Laboratory, Paris Descartes University, CNRS UMR 8250, Sorbonne Paris Cité, F-75006 Paris, France; bruno.gasnier@parisdescartes.fr corinne.sagne@parisdescartes.fr.ORCID 0000-0003-4458-6296
Corinne SagnéNeurophotonics Laboratory, Paris Descartes University, CNRS UMR 8250, Sorbonne Paris Cité, F-75006 Paris, France; bruno.gasnier@parisdescartes.fr corinne.sagne@parisdescartes.fr.
Délégation Paris 5 · FRUniversity of Namur · BE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lysosomes degrade cellular components sequestered by autophagy or extracellular material internalized by endocytosis and phagocytosis. The macromolecule building blocks released by lysosomal hydrolysis are then exported to the cytosol by lysosomal transporters, which remain undercharacterized. In this study, we designed an in situ assay of lysosomal amino acid export based on the transcription factor EB (TFEB), a master regulator of lysosomal biogenesis that detects lysosomal storage. This assay was used to screen candidate lysosomal transporters, leading to the identification of sodium-coupled neutral amino acid transporter 7 (SNAT7), encoded by the SLC38A7 gene, as a lysosomal transporter highly selective for glutamine and asparagine. Cell fractionation confirmed the lysosomal localization of SNAT7, and flux measurements confirmed its substrate selectivity and showed a strong activation by the lysosomal pH gradient. Interestingly, gene silencing or editing experiments revealed that SNAT7 is the primary permeation pathway for glutamine across the lysosomal membrane and it is required for growth of cancer cells in a low free-glutamine environment, when macropinocytosis and lysosomal degradation of extracellular proteins are used as an alternative source of amino acids. SNAT7 may, thus, represent a novel target for glutamine-related anticancer therapies.

Indexed as

Amino Acid Transport Systems, NeutralGlutamineHeLa CellsHumansIntracellular MembranesLysosomesNeoplasm ProteinsNeoplasmsTumor MicroenvironmentAmino Acid Transport Systems, NeutralGlutamineNeoplasm Proteinscancercell nutritionglutaminelysosometransporter

Identifiers

PMID28416685
PMCPMC5422790
OpenAlexW2606268808

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.