Evidence map›Paper›PMID 34706237›Full record

ArticleCell reports2021

Structural and compositional diversity in the kainate receptor family.

Purushotham Selvakumar, Joon Lee, Nandish Khanra, Changhao He, Hermany Munguba, Lisa Kiese, Johannes Broichhagen, Andreas Reiner, Joshua Levitz, Joel R Meyerson

Open access · goldAbstract read
In one paragraph

Article in Cell reports, 2021. 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
2.3field-weighted citation impact, top 11% 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, 41 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Structure and gating of kainate receptors.Frontiers in pharmacology · 2025
    Review
  10. Article
  11. Article
  12. Review
  13. Kainate Receptor Antagonists: Recent Advances and Therapeutic Perspective.International journal of molecular sciences · 2023
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Review
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 2 countries.

Purushotham SelvakumarDepartment of Physiology and Biophysics, Weill Cornell Medical College, New York, NY 10065, USA.
Joon LeeDepartment of Biochemistry, Weill Cornell Medical College, New York, NY 10065, USA.
Nandish KhanraDepartment of Physiology and Biophysics, Weill Cornell Medical College, New York, NY 10065, USA.
Changhao HeDepartment of Physiology and Biophysics, Weill Cornell Medical College, New York, NY 10065, USA.
Hermany MungubaDepartment of Biochemistry, Weill Cornell Medical College, New York, NY 10065, USA.
Lisa KieseDepartment of Biology and Biotechnology, Ruhr University Bochum, Bochum, Germany.
Johannes BroichhagenLeibniz-Forschungsinstitut für Molekulare Pharmakologie, 13125 Berlin, Germany.
Andreas ReinerDepartment of Biology and Biotechnology, Ruhr University Bochum, Bochum, Germany.
Joshua LevitzDepartment of Biochemistry, Weill Cornell Medical College, New York, NY 10065, USA. Electronic address: jtl2003@med.cornell.edu.
Joel R MeyersonDepartment of Physiology and Biophysics, Weill Cornell Medical College, New York, NY 10065, USA. Electronic address: jrm2008@med.cornell.edu.
Cornell University · USRuhr University Bochum · DELeibniz-Forschungsinstitut für Molekulare Pharmakologie · DE

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
Molecular Mechanisms of Synaptic G Protein-Coupled ReceptorsR35GM124731 · NIGMS · WEILL MEDICAL COLL OF CORNELL UNIV · PI LEVITZ, JOSHUA · 2017 to 2021
$2.1M
Molecular Mechanisms, Modulation, and Synaptic Organization of Kainate ReceptorsR35GM142662 · NIGMS · WEILL MEDICAL COLL OF CORNELL UNIV · PI LEVITZ, JOSHUA · 2021 to 2022
$787k
NIGMS NIH HHS P41 GM103310NIGMS NIH HHS R35 GM124731NIGMS NIH HHS R35 GM142662
6 · The paper itself

Abstract

The kainate receptors (KARs) are members of the ionotropic glutamate receptor family and assemble into tetramers from a pool of five subunit types (GluK1-5). Each subunit confers distinct functional properties to a receptor, but the compositional and stoichiometric diversity of KAR tetramers is not well understood. To address this, we first solve the structure of the GluK1 homomer, which enables a systematic assessment of structural compatibility among KAR subunits. Next, we analyze single-cell RNA sequencing data, which reveal extreme diversity in the combinations of two or more KAR subunits co-expressed within the same cell. We then investigate the composition of individual receptor complexes using single-molecule fluorescence techniques and find that di-heteromers assembled from GluK1, GluK2, or GluK3 can form with all possible stoichiometries, while GluK1/K5, GluK2/K5, and GluK3/K5 can form 3:1 or 2:2 complexes. Finally, using three-color single-molecule imaging, we discover that KARs can form tri- and tetra-heteromers.

Indexed as

Protein MultimerizationCell MembraneHEK293 CellsHumansKainic Acid ReceptorsProtein SubunitsKainic Acid ReceptorsProtein Subunitscryo-electron microscopyiGluRskainate receptorssingle-cell RNA sequencingsingle-molecule Förster resonance energy transfersingle-molecule pull-down

Identifiers

PMID34706237
PMCPMC8581553
OpenAlexW3208642215

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.