Evidence map›Paper›PMID 12748860›Full record

ReviewPflugers Archiv : European journal of physiology2004

The SLC36 family: proton-coupled transporters for the absorption of selected amino acids from extracellular and intracellular proteolysis.

Michael Boll, Hannelore Daniel, Bruno Gasnier

Abstract readReview
PubMed Publisher
In one paragraph

Review in Pflugers Archiv : European journal of physiology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
6.0field-weighted citation impact, top 3% 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

44 citing papers in PubMed, 108 citations in OpenAlex.

  1. Trial
  2. Stage-Specific H3K14 and H3K23 Succinylation Orchestrates Insect Metamorphosis and Oogenesis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  3. Article
  4. Comparative Gut Proteome ofMicroorganisms · 2025
    Article
  5. Glycine: The Smallest Anti-Inflammatory Micronutrient.International journal of molecular sciences · 2023
    Review
  6. Article
  7. Review
  8. Article
  9. Article
  10. Review
  11. Preclinical Evaluation ofJournal of nuclear medicine : official publication, Society of Nuclear Medicine · 2017
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. The Concise Guide to PHARMACOLOGY 2013/14: transporters.British journal of pharmacology · 2013
    Article
  17. Review
  18. Article
  19. Article
  20. 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

3 authors at 2 institutions in 2 countries.

Michael BollMolecular Nutrition Unit, Institute of Nutritional Sciences, Technical University of Munich, Hochfeldweg 2, 85350, Freising-Weihenstephan, Germany. boll@wzw.tum.de
Hannelore Daniel
Bruno Gasnier
Technical University of Munich · DEInstitut de Biologie Physico-Chimique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Whilst Na(+) has replaced H(+) as a major transport driving force at the plasma membrane of animal cells, the evolutionarily older H(+)-driven systems persist on endomembranes and at the plasma membrane of specialized cells. The first member of the SLC36 family, present in both intracellular and plasma membranes, was identified independently as a lysosomal amino acid transporter (LYAAT1) responsible for the export of lysosomal proteolysis products into the cytosol and as a proton/amino acid transporter (PAT1) responsible for the absorption of amino acids in the gut. In addition to LYAAT1/PAT1, the family comprises another characterized member, PAT2, and two orphan transporters. Both PAT1 and PAT2 mediate 1:1 symport of protons and small neutral amino acids such as glycine, alanine, and proline. Their mRNAs are broadly and differentially expressed in mammalian tissues. The PAT1 protein localizes to lysosomes in brain neurons, but is also found in the apical membrane of intestinal epithelial cells with a role in the absorption of amino acids from luminal protein digestion. In both cases, protons supplied by the lysosomal H(+)-ATPase or by the acidic microclimate of the brush border membrane drive transport of the amino acids into the cytosol. The subcellular localization and physiological role of PAT2 have still to be determined. SLC36 transporters are related distantly to other proton-coupled amino acid transporters, such as the vesicular neurotransmitter transporter VIAAT/VGAT (SLC32) and system N transporters (SLC38 family).

Indexed as

Amino AcidsAmino Acid Transport SystemsAnimalsBiological TransportExtracellular SpaceHumansLysosomesMultigene FamilyProtonsAmino AcidsAmino Acid Transport SystemsProtons

Identifiers

PMID12748860
OpenAlexW2017781065

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.