Evidence map›Paper›PMID 19147495›Full record

ArticleThe Journal of biological chemistry2009

Synaptic Vesicle Protein NTT4/XT1 (SLC6A17) Catalyzes Na+-coupled Neutral Amino Acid Transport.

Kimberly A Zaia, Richard J Reimer

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
0.7field-weighted citation impact, top 32% 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

31 citing papers in PubMed, 54 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Computational and structural biotechnology journal · 2024
    Article
  7. Article
  8. Article
  9. Article
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  11. Review
  12. Review
  13. Article
  14. Chloride-dependent conformational changes in the GlyT1 glycine transporter.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  15. Heteromeric Solute Carriers: Function, Structure, Pathology and Pharmacology.Advances in experimental medicine and biology · 2021
    Review
  16. Amino Acid Transporter SLC6A14 (ATBFrontiers in cell and developmental biology · 2020
    Review
  17. Amino Acid Transport Defects in Human Inherited Metabolic Disorders.International journal of molecular sciences · 2019
    Review
  18. Article
  19. Article
  20. Article
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

2 authors at 1 institution in 1 country.

Kimberly A ZaiaDepartment of Neurology and Neurological Sciences and Neuroscience Graduate Program, Stanford University, Stanford, California 94305, USA.
Richard J Reimer
Stanford University · US

Funding

Molecular Mechanisms of Vesicular Glutamate TransportK02NS045634 · NINDS · STANFORD UNIVERSITY · PI REIMER, RICHARD J · 2003 to 2007
$731k
NINDS NIH HHS K02 NS045634
6 · The paper itself

Abstract

The SLC6 family of structurally related, Na(+)-dependent transporter proteins is responsible for presynaptic reuptake of the majority of neurotransmitters. Within this family are a number of orphan transporters, including NTT4/XT1 (SLC6A17), a protein first identified over 15 years ago. NTT4/XT1 is expressed exclusively in the nervous system and specifically on synaptic vesicles in glutamatergic and some GABAergic neurons. Despite extensive efforts by a number of groups, no substrate has been reported for NTT4/XT1. Here we use a combination of molecular manipulations to increase expression of the NTT4/XT1 protein at the plasma membrane and to directly demonstrate that it catalyzes neutral amino acid transport. The substrate profile of the NTT4/XT1-dependent activity is similar to that of the closely related B(0)AT2/SBAT1 (SLC6A15), including a submillimolar apparent affinity for proline and leucine and a low millimolar apparent affinity for glutamine. The transport activity is Na(+)-dependent and Cl(-)-independent and is inhibited by low pH as is SLC6A15, suggesting redundant roles for these proteins. This characterization of NTT4/XT1 offers important insights into neurotransmitter metabolism as well as the mechanistic differences among the structurally related, but functionally divergent, SLC6 proteins.

Indexed as

Amino Acids, NeutralAmino Acid Transport Systems, NeutralAnimalsBiological TransportCatalysisCell LineCell MembraneHumansNerve Tissue ProteinsNeurotransmitter AgentsPC12 CellsPlasma Membrane Neurotransmitter Transport ProteinsRatsSodiumSynaptic VesiclesAmino Acids, NeutralAmino Acid Transport Systems, NeutralNerve Tissue ProteinsNeurotransmitter AgentsPlasma Membrane Neurotransmitter Transport ProteinsSLC6A15 protein, humanSlc6a17 protein, ratSodium

Identifiers

PMID19147495
PMCPMC2659202
OpenAlexW2002400344

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.