Evidence map›Paper›PMID 22778417›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2012

Sushi domains confer distinct trafficking profiles on GABAB receptors.

Saad Hannan, Megan E Wilkins, Trevor G Smart

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
0.9field-weighted citation impact, top 32% 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

25 citing papers in PubMed, 36 citations in OpenAlex.

  1. Monoallelic de novoScience advances · 2024
    Article
  2. Article
  3. Article
  4. The role of GABAFrontiers in endocrinology · 2023
    Review
  5. CaInternational journal of molecular sciences · 2022
    Review
  6. Structural Basis of GABACurrent topics in behavioral neurosciences · 2022
    Review
  7. Review
  8. Mechanisms and Regulation of Neuronal GABACurrent topics in behavioral neurosciences · 2022
    Review
  9. GABACurrent topics in behavioral neurosciences · 2022
    Review
  10. Review
  11. Article
  12. Review
  13. Article
  14. Complex formation of APP with GABANature communications · 2019
    Article
  15. Review
  16. Cell surface expression of homomeric GABAThe Journal of biological chemistry · 2018
    Article
  17. Article
  18. Article
  19. Article
  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

3 authors at 1 institution in 1 country.

Saad HannanDepartment of Neuroscience, Physiology, and Pharmacology, University College London, London, United Kingdom.
Megan E Wilkins
Trevor G Smart
University College London · GB

Funding

Biotechnology and Biological Sciences Research CouncilMedical Research Council G0601529
6 · The paper itself

Abstract

GABA(B) receptors mediate slow inhibitory neurotransmission in the brain and feature during excitatory synaptic plasticity, as well as various neurological conditions. These receptors are obligate heterodimers composed of GABA(B)R1 and R2 subunits. The two predominant R1 isoforms differ by the presence of two complement control protein modules or Sushi domains (SDs) in the N terminus of R1a. By using live imaging, with an α-bungarotoxin-binding site (BBS) and fluorophore-linked bungarotoxin, we studied how R2 stabilizes R1b subunits at the cell surface. Heterodimerization with R2 reduced the rate of internalization of R1b, compared with R1b homomers. However, R1aR2 heteromers exhibited increased cell surface stability compared with R1bR2 receptors in hippocampal neurons, suggesting that for receptors containing the R1a subunit, the SDs play an additional role in the surface stability of GABA(B) receptors. Both SDs were necessary to increase the stability of R1aR2 because single deletions caused the receptors to be internalized at the same rate and extent as R1bR2 receptors. Consistent with these findings, a chimera formed from the metabotropic glutamate receptor (mGluR)2 and the SDs from R1a increased the surface stability of mGluR2. These results suggest a role for SDs in stabilizing cell surface receptors that could impart different pre- and postsynaptic trafficking itineraries on GABA(B) receptors, thereby contributing to their physiological and pathological roles.

Indexed as

BungarotoxinsHEK293 CellsHippocampusHumansImage Processing, Computer-AssistedPatch-Clamp TechniquesProtein IsoformsProtein MultimerizationProtein StabilityProtein Structure, TertiaryProtein SubunitsProtein TransportReceptors, GABA-BReceptors, Metabotropic GlutamateRecombinant Fusion ProteinsSynaptic TransmissionBungarotoxinsmetabotropic glutamate receptor 2Protein IsoformsProtein SubunitsReceptors, GABA-BReceptors, Metabotropic GlutamateRecombinant Fusion Proteins

Identifiers

PMID22778417
PMCPMC3409743
OpenAlexW1983341397

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.