Evidence map›Paper›PMID 19478081›Full record

ArticleThe Journal of biological chemistry2009

Orphan transporter SLC6A18 is renal neutral amino acid transporter B0AT3.

Dustin Singer, Simone M R Camargo, Katja Huggel, Elisa Romeo, Ursula Danilczyk, Keiji Kuba, Serge Chesnov, Marc G Caron, Josef M Penninger, Francois Verrey

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 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

36 citing papers in PubMed, 68 citations in OpenAlex.

  1. Review
  2. A Urinary Three-Metabolite Signature Enables Noninvasive Identification of Patients with High-Risk Ovarian Cancer.Clinical cancer research : an official journal of the American Association for Cancer Research · 2026
    Article
  3. Article
  4. ACE2: Friend or Foe in Post-COVID-19 Neurodegeneration?International journal of molecular sciences · 2025
    Review
  5. Article
  6. Review
  7. Review
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  9. Article
  10. Article
  11. Review
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  15. Review
  16. Review
  17. Review
  18. Chloride-dependent conformational changes in the GlyT1 glycine transporter.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  19. Article
  20. Heteromeric Solute Carriers: Function, Structure, Pathology and Pharmacology.Advances in experimental medicine and biology · 2021
    Review
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

10 authors at 5 institutions in 3 countries.

Dustin SingerInstitute of Physiology and Center for Integrative Human Physiology, University of Zürich, 8057 Zürich, Switzerland.
Simone M R Camargo
Katja Huggel
Elisa Romeo
Ursula Danilczyk
Keiji Kuba
Serge Chesnov
Marc G Caron
Josef M Penninger
Francois Verrey
Austrian Academy of Sciences · ATSwiss Integrative Center for Human Health · CHUniversity of Zurich · CHDuke University Hospital · USETH Zurich · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The orphan transporter Slc6a18 (XT2) is highly expressed at the luminal membrane of kidney proximal tubules and displays approximately 50% identity with Slc6a19 (B(0)AT1), which is the main neutral amino acid transporter in both kidney and small intestine. As yet, the amino acid transport function of XT2 has only been experimentally supported by the urinary glycine loss observed in xt2 null mice. We report here that in Xenopus laevis oocytes, co-expressed ACE2 (angiotensin-converting enzyme 2) associates with XT2 and reveals its function as a Na(+)- and Cl(-)-de pend ent neutral amino acid transporter. In contrast to its association with ACE2 observed in Xenopus laevis oocytes, our experiments with ace2 and collectrin null mice demonstrate that in vivo it is Collectrin, a smaller homologue of ACE2, that is required for functional expression of XT2 in kidney. To assess the function of XT2 in vivo, we reanalyzed its knock-out mouse model after more than 10 generations of backcrossing into C57BL/6 background. In addition to the previously published glycinuria, we observed a urinary loss of several other amino acids, in particular beta-branched and small neutral ones. Using telemetry, we confirmed the previously described link of XT2 absence with hypertension but only in physically restrained animals. Taken together, our data indicate that the formerly orphan transporter XT2 functions as a sodium and chloride-de pend ent neutral amino acid transporter that we propose to rename B(0)AT3.

Indexed as

Amino AcidsAmino Acid Transport Systems, NeutralAngiotensin-Converting Enzyme 2AnimalsBiological TransportBlood PressureGene ExpressionMembrane GlycoproteinsMembrane Transport ProteinsMiceMice, Inbred C57BLMice, KnockoutOocytesPeptidyl-Dipeptidase APlasma Membrane Neurotransmitter Transport ProteinsRespirationACE2 protein, humanAce2 protein, mouseAmino AcidsAmino Acid Transport Systems, NeutralAngiotensin-Converting Enzyme 2Membrane GlycoproteinsMembrane Transport ProteinsPeptidyl-Dipeptidase APlasma Membrane Neurotransmitter Transport ProteinsTmem27 protein, mouseXtrp2 protein, mouse

Identifiers

PMID19478081
PMCPMC2740421
OpenAlexW1983421391

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.