Evidence map›Paper›PMID 37142617›Full record

ArticleNature communications2023

Symport and antiport mechanisms of human glutamate transporters.

Biao Qiu, Olga Boudker

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
3.7field-weighted citation impact, top 6% 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

20 citing papers in PubMed, 25 citations in OpenAlex.

  1. Review
  2. Review
  3. Multimodal dynamics control activity of a glial glutamate transporter.bioRxiv : the preprint server for biology · 2026
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Structural basis of excitatory amino acid transporter 3 substrate recognition.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Cation-Binding of Glutamate in Aqueous Solution.The journal of physical chemistry. B · 2024
    Article
  18. Identification of the potassium-binding site in serotonin transporter.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  19. Review
  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

2 authors at 2 institutions in 1 country.

Biao QiuDepartment of Physiology & Biophysics, Weill Cornell Medicine, 1300 York Ave, New York, NY, 10021, USA. biq2001@med.cornell.edu.ORCID 0000-0003-3633-5091
Olga BoudkerDepartment of Physiology & Biophysics, Weill Cornell Medicine, 1300 York Ave, New York, NY, 10021, USA. olb2003@med.cornell.edu.ORCID 0000-0001-6965-0851
Cornell University · USHoward Hughes Medical Institute · US

Funding

TRD #3: An automated and streamlined pipeline for in-situ molecular microscopyP41GM103310 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI DE MARCO, ALEX, KIEFT, JEFFREY S · 2012 to 2021
$14.7M
The structural dynamics of a glutamate transporter homologueR37NS085318 · NINDS · WEILL MEDICAL COLL OF CORNELL UNIV · PI BOUDKER, OLGA · 2014 to 2020
$4.3M
Dual-Beam Scanning Electron Microscope for New York Structural Biology CenterS10RR029300 · NCRR · NEW YORK STRUCTURAL BIOLOGY CENTER · PI STOKES, DAVID L. · 2010 to 2010
$2.0M
Ion coupling, permeation, and regulation in glutamate transportersR37NS134865 · NINDS · WEILL MEDICAL COLL OF CORNELL UNIV · PI Olga Boudker · 2024 to 2026
$1.7M
Acquisition of Detector for JEOL 3200 FSC Electron MicroscopeS10OD019994 · OD · NEW YORK STRUCTURAL BIOLOGY CENTER · PI CARRAGHER, BRIDGET OLIVIA · 2015 to 2015
$600k
NCRR NIH HHS S10 RR029300NIGMS NIH HHS P41 GM103310NIH HHS S10 OD019994NINDS NIH HHS R37 NS085318NINDS NIH HHS R37 NS134865U.S. Department of Health & Human Services | NIH | National Institute of Neurological Disorders and Stroke (NINDS) R37NS085318
6 · The paper itself

Abstract

Excitatory amino acid transporters (EAATs) uptake glutamate into glial cells and neurons. EAATs achieve million-fold transmitter gradients by symporting it with three sodium ions and a proton, and countertransporting a potassium ion via an elevator mechanism. Despite the availability of structures, the symport and antiport mechanisms still need to be clarified. We report high-resolution cryo-EM structures of human EAAT3 bound to the neurotransmitter glutamate with symported ions, potassium ions, sodium ions alone, or without ligands. We show that an evolutionarily conserved occluded translocation intermediate has a dramatically higher affinity for the neurotransmitter and the countertransported potassium ion than outward- or inward-facing transporters and plays a crucial role in ion coupling. We propose a comprehensive ion coupling mechanism involving a choreographed interplay between bound solutes, conformations of conserved amino acid motifs, and movements of the gating hairpin and the substrate-binding domain.

Indexed as

Amino Acid Transport System X-AGGlutamic AcidHumansIonsIon TransportPotassiumSodiumAmino Acid Transport System X-AGGlutamic AcidIonsPotassiumSodium

Identifiers

PMID37142617
PMCPMC10160106
OpenAlexW4372335198

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.