Evidence map›Paper›PMID 18252709›Full record

ArticleThe Journal of biological chemistry2008

Glycine transporter dimers: evidence for occurrence in the plasma membrane.

Ingo Bartholomäus, Laura Milan-Lobo, Annette Nicke, Sébastien Dutertre, Hanne Hastrup, Alok Jha, Ulrik Gether, Harald H Sitte, Heinrich Betz, Volker Eulenburg

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
4.0field-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

38 citing papers in PubMed, 63 citations in OpenAlex.

  1. Trial
  2. Trial
  3. Review
  4. Article
  5. A New GlyT2 Variant Associated with Hyperekplexia.International journal of molecular sciences · 2025
    Article
  6. Article
  7. Article
  8. Structures and membrane interactions of native serotonin transporter in complexes with psychostimulants.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  9. Article
  10. Article
  11. Article
  12. SLC6 transporter oligomerization.Journal of neurochemistry · 2021
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Transporter oligomerization: form and function.Biochemical Society transactions · 2016
    Review
  19. Amphetamine action at the cocaine- and antidepressant-sensitive serotonin transporter is modulated by αCaMKII.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2015
    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

10 authors at 3 institutions in 3 countries.

Ingo BartholomäusDepartment of Neurochemistry, Max Planck Institute for Brain Research, Deutschordenstrasse 46, 60529 Frankfurt, Germany.
Laura Milan-Lobo
Annette Nicke
Sébastien Dutertre
Hanne Hastrup
Alok Jha
Ulrik Gether
Harald H Sitte
Heinrich Betz
Volker Eulenburg
Max Planck Institute for Brain Research · DEMedical University of Vienna · ATUniversity of Copenhagen · DK

Funding

Austrian Science Fund FWF P 18706
6 · The paper itself

Abstract

Different Na(+)/Cl(-)-dependent neurotransmitter transporters of the SLC6a family have been shown to form dimers or oligomers in both intracellular compartments and at the cell surface. In contrast, the glycine transporters (GlyTs) GlyT1 and -2 have been reported to exist as monomers in the plasma membrane based on hydrodynamic and native gel electrophoretic studies. Here, we used cysteine substitution and oxidative cross-linking to show that of GlyT1 and GlyT2 also form dimeric complexes within the plasma membrane. GlyT oligomerization at the cell surface was confirmed for both GlyT1 and GlyT2 by fluorescence resonance energy transfer microscopy. Endoglycosidase treatment and surface biotinylation further revealed that complex-glycosylated GlyTs form dimers located at the cell surface. Furthermore, substitution of tryptophan 469 of GlyT2 by an arginine generated a transporter deficient in dimerization that was retained intracellulary. Based on these results and GlyT structures modeled by using the crystal structure of the bacterial homolog LeuT(Aa), as a template, residues located within the extracellular loop 3 and at the beginning of transmembrane domain 6 are proposed to contribute to the dimerization interface of GlyTs.

Indexed as

DimerizationGene Expression RegulationAmino Acid SequenceBiological TransportCell MembraneCross-Linking ReagentsFluorescence Resonance Energy TransferGlycineGlycoside HydrolasesHumansModels, BiologicalModels, MolecularMolecular Sequence DataProtein ConformationCross-Linking ReagentsGlycineGlycoside Hydrolases

Identifiers

PMID18252709
PMCPMC4503265
OpenAlexW1972342888

What OpenQuestion holds

Textmetadata
LicenceTDM
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.