Evidence map›Paper›PMID 11390972›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2001

Identification and characterization of a lysosomal transporter for small neutral amino acids.

C Sagné, C Agulhon, P Ravassard, M Darmon, M Hamon, S El Mestikawy, B Gasnier, B Giros

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 90 papers.

0numbers the graph read from it
0cells of the map it votes in
90citing papers in PubMed
7.6field-weighted citation impact, top 2% 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

90 citing papers in PubMed, 232 citations in OpenAlex.

  1. Review
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  8. The ion channels of endomembranes.Physiological reviews · 2024
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  9. Article
  10. Review
  11. Article
  12. Article
  13. The transcriptomic response ofFrontiers in cellular and infection microbiology · 2023
    Article
  14. Review
  15. Lysosomal solute and water transport.The Journal of cell biology · 2022
    Review
  16. Review
  17. Article
  18. Article
  19. Review
  20. Article

30 more citing papers are in PubMed but not listed here.

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

8 authors at 1 institution in 1 country.

C SagnéInstitut National de la Santé et de la Recherche Médicale U-513, CHU Henri Mondor, 8 Rue du Général Sarrail, 94010 Créteil Cedex, France. sagne@im3.inserm.fr
C Agulhon
P Ravassard
M Darmon
M Hamon
S El Mestikawy
B Gasnier
B Giros
Institut de Biologie Physico-Chimique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In eukaryotic cells, lysosomes represent a major site for macromolecule degradation. Hydrolysis products are eventually exported from this acidic organelle into the cytosol through specific transporters. Impairment of this process at either the hydrolysis or the efflux step is responsible of several lysosomal storage diseases. However, most lysosomal transporters, although biochemically characterized, remain unknown at the molecular level. In this study, we report the molecular and functional characterization of a lysosomal amino acid transporter (LYAAT-1), remotely related to a family of H+-coupled plasma membrane and synaptic vesicle amino acid transporters. LYAAT-1 is expressed in most rat tissues, with highest levels in the brain where it is present in neurons. Upon overexpression in COS-7 cells, the recombinant protein mediates the accumulation of neutral amino acids, such as gamma-aminobutyric acid, l-alanine, and l-proline, through an H+/amino acid symport. Confocal microscopy on brain sections revealed that this transporter colocalizes with cathepsin D, an established lysosomal marker. LYAAT-1 thus appears as a lysosomal transporter that actively exports neutral amino acids from lysosomes by chemiosmotic coupling to the H+-ATPase of these organelles. Homology searching in eukaryotic genomes suggests that LYAAT-1 defines a subgroup of lysosomal transporters in the amino acid/auxin permease family.

Indexed as

Amino Acid Transport SystemsAmino Acid Transport Systems, NeutralAlanineAmino Acid SequenceAmino Acids, NeutralAnimalsBrainCaenorhabditis elegansCarrier ProteinsCell LineCerebral CortexCloning, MolecularDrosophila melanogasterEvolution, Moleculargamma-Aminobutyric AcidHippocampusAlanineAmino Acids, NeutralAmino Acid Transport SystemsAmino Acid Transport Systems, NeutralCarrier Proteinsgamma-Aminobutyric AcidProlineRecombinant ProteinsSlc36a1 protein, ratSymporters

Identifiers

PMID11390972
PMCPMC34647
OpenAlexW1987066803

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.