Evidence map›Paper›PMID 11171971›Full record

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

Surface-localized glycine transporters 1 and 2 function as monomeric proteins in Xenopus oocytes.

M Horiuchi, A Nicke, J Gomeza, A Aschrafi, G Schmalzing, H Betz

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 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

12 citing papers in PubMed, 51 citations in OpenAlex.

  1. 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
  2. Review
  3. Article
  4. SLC6 transporter oligomerization.Journal of neurochemistry · 2021
    Review
  5. Vesicular and plasma membrane transporters for neurotransmitters.Cold Spring Harbor perspectives in biology · 2012
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. 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

6 authors at 2 institutions in 1 country.

M HoriuchiDepartment of Neurochemistry, Max Planck Institute for Brain Research, Deutschordenstrasse 46, D-60528 Frankfurt am Main, Germany.
A Nicke
J Gomeza
A Aschrafi
G Schmalzing
H Betz
Max Planck Institute for Brain Research · DEGoethe University Frankfurt · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Na(+)/Cl(-)-dependent neurotransmitter transporters form a superfamily of transmembrane proteins that share 12 membrane-spanning regions. To gain information about the quaternary structure of these transporter proteins, we heterologously expressed the glial glycine transporter GlyT1 and its neuronal homolog GlyT2 in Xenopus oocytes. By using metabolic labeling with [(35)S]methionine or surface labeling with a plasma membrane impermeable reagent followed by affinity purification, we separately analyzed the total cellular pools of newly synthesized GlyTs and its functional plasma membrane-bound fractions. Upon blue native gel electrophoresis, the surface-localized transporter proteins were found to exist exclusively in complex-glycosylated monomeric form, whereas a significant fraction of the intracellular GlyT1 and GlyT2 was core-glycosylated and oligomeric. In contrast, even after treatment with the crosslinker glutaraldehyde, surface GlyTs failed to migrate as oligomeric proteins. These results indicate that plasma membrane-bound GlyT1 and GlyT2 are monomeric proteins. Thus, Na(+)/Cl(-)-dependent neurotransmitter transporters do not require oligomerization for substrate translocation.

Indexed as

Amino Acid Transport Systems, NeutralAnimalsCarrier ProteinsCell MembraneGlycineGlycine Plasma Membrane Transport ProteinsMembrane ProteinsOligopeptidesOocytesRecombinant Fusion ProteinsXenopus laevisAmino Acid Transport Systems, NeutralCarrier ProteinsGlycineGlycine Plasma Membrane Transport ProteinsMembrane ProteinsOligopeptidesRecombinant Fusion Proteins

Identifiers

PMID11171971
PMCPMC29277
OpenAlexW2167210425

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.