Evidence map›Paper›PMID 11278474›Full record

ArticleThe Journal of biological chemistry2001

The glial and the neuronal glycine transporters differ in their reactivity to sulfhydryl reagents.

M J Roux, R Martinez-Maza, A Le Goff, B Lopez-Corcuera, C Aragon, S Supplisson

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.8field-weighted citation impact, top 18% 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

13 citing papers in PubMed, 32 citations in OpenAlex.

  1. Trial
  2. Article
  3. Review
  4. Article
  5. Flux coupling, not specificity, shapes the transport and phylogeny of SLC6 glycine transporters.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. The zebrafish shocked gene encodes a glycine transporter and is essential for the function of early neural circuits in the CNS.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2005
    Article
  13. 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 1 institution in 1 country.

M J RouxLaboratoire de Neurobiologie, Unité Mixte de Recherche 8544, Centre National de la Recherche Scientifique, Ecole Normale Supérieure, 46 rue d'Ulm, 75230 Paris cedex 05, France.
R Martinez-Maza
A Le Goff
B Lopez-Corcuera
C Aragon
S Supplisson
Centro de Biología Molecular Severo Ochoa · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The neuronal (GlyT2) and glial (GlyT1) glycine transporters, two members of the Na(+)/Cl(-)-dependent neurotransmitter transporter superfamily, differ by many aspects, such as substrate specificity and Na(+) coupling. We have characterized under voltage clamp their reactivity toward the membrane impermeant sulfhydryl reagent [2-(trimethylammonium)-ethyl]-methanethiosulfonate (MTSET). In Xenopus oocytes expressing GlyT1b, application of MTSET reduced to the same extent the Na(+)-dependent charge movement, the glycine-evoked current, and the glycine uptake, indicating a complete inactivation of the transporters following cysteine modification. In contrast, this compound had no detectable effect on the glycine uptake and the glycine-evoked current of GlyT2a. The sensitivities to MTSET of the two transporters can be permutated by suppressing a cysteine (C62A) in the first extracellular loop (EL1) of GlyT1b and introducing one at the equivalent position in GlyT2a, either by point mutation (A223C) or by swapping the EL1 sequence (GlyT1b-EL1 and GlyT2a-EL1) resulting in AFQ <--> CYR modification. Inactivation by MTSET was five times faster in GlyT2a-A223C than in GlyT2a-EL1 or GlyT1b, suggesting that the arginine in position +2 reduced the cysteine reactivity. Protection assays indicate that EL1 cysteines are less accessible in the presence of all co-transported substrates: Na(+), Cl(-), and glycine. Application of dithioerythritol reverses the inactivation by MTSET of the sensitive transporters. Together, these results indicate that EL1 conformation differs between GlyT1b and GlyT2a and is modified by substrate binding and translocation.

Indexed as

Amino Acid Transport Systems, NeutralAmino Acid SequenceAnimalsCarrier ProteinsGlycine Plasma Membrane Transport ProteinsMesylatesMolecular Sequence DataNeurogliaNeuronsOrgan SpecificityPatch-Clamp TechniquesSulfhydryl ReagentsXenopus(2-(trimethylammonium)ethyl)methanethiosulfonateAmino Acid Transport Systems, NeutralCarrier ProteinsGlycine Plasma Membrane Transport ProteinsMesylatesSulfhydryl Reagents

Identifiers

PMID11278474
PMCPMC2375918
OpenAlexW2079382471

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.