Evidence map›Paper›PMID 16128593›Full record

ArticleBiochemistry2005

Individual subunits of the glutamate transporter EAAC1 homotrimer function independently of each other.

Christof Grewer, Poonam Balani, Christian Weidenfeller, Thorsten Bartusel, Zhen Tao, Thomas Rauen

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 87 papers.

0numbers the graph read from it
0cells of the map it votes in
87citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

87 citing papers in PubMed, 145 citations in OpenAlex.

  1. Article
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  9. Review
  10. Article
  11. Kinetic mechanism of NaCommunications biology · 2021
    Article
  12. Article
  13. Article
  14. Cellular Physiology and Pathophysiology of EAAT Anion Channels.Frontiers in cellular neuroscience · 2021
    Review
  15. Review
  16. Article
  17. Elevator-type mechanisms of membrane transport.Biochemical Society transactions · 2020
    Review
  18. Review
  19. Article
  20. Article

27 more citing papers are in PubMed but not listed here.

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 3 institutions in 2 countries.

Christof GrewerUniversity of Miami School of Medicine, 1600 NW 10th Avenue, Miami, Florida 33136, USA. cgrewer@med.miami.edu
Poonam Balani
Christian Weidenfeller
Thorsten Bartusel
Zhen Tao
Thomas Rauen
Osnabrück University · DEUniversity of Miami · USUniversity of Münster · DE

Funding

Molecular Basis of Glutamate TransportR01NS049335 · NINDS · UNIVERSITY OF MIAMI SCHOOL OF MEDICINE · PI GREWER, CHRISTOF THEODOR · 2004 to 2012
$2.0M
NINDS NIH HHS R01-NS0493NINDS NIH HHS R01 NS049335
6 · The paper itself

Abstract

Glutamate transporters are thought to be assembled as trimers of identical subunits that line a central hole, possibly the permeation pathway for anions. Here, we have tested the effect of multimerization on the transporter function. To do so, we coexpressed EAAC1(WT) with the mutant transporter EAAC1(R446Q), which transports glutamine but not glutamate. Application of 50 microM glutamate or 50 microM glutamine to cells coexpressing similar numbers of both transporters resulted in anion currents of 165 and 130 pA, respectively. Application of both substrates at the same time generated an anion current of 297 pA, demonstrating that the currents catalyzed by the wild-type and mutant transporter subunits are purely additive. This result is unexpected for anion permeation through a central pore but could be explained by anion permeation through independently functioning subunits. To further test the subunit independence, we coexpressed EAAC1(WT) and EAAC1(H295K), a transporter with a 90-fold reduced glutamate affinity as compared to EAAC1(WT), and determined the glutamate concentration dependence of currents of the mixed transporter population. The data were consistent with two independent populations of transporters with apparent glutamate affinities similar to those of EAAC1(H295K) and EAAC1(WT), respectively. Finally, we coexpressed EAAC1(WT) with the pH-independent mutant transporter EAAC1(E373Q), showing two independent populations of transporters, one being pH-dependent and the other being pH-independent. In conclusion, we propose that EAAC1 assembles as trimers of identical subunits but that the individual subunits in the trimer function independently of each other.

Indexed as

AlanineAmino Acid SubstitutionAnimalsAspartic AcidDose-Response Relationship, DrugExcitatory Amino Acid Transporter 3Glutamic AcidGlutamineHumansMutagenesis, Site-DirectedProtein SubunitsRatsAlanineAspartic AcidbenzyloxyaspartateExcitatory Amino Acid Transporter 3Glutamic AcidGlutamineProtein SubunitsSlc1a1 protein, rat

Identifiers

PMID16128593
PMCPMC2459315
OpenAlexW2000632273

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.