Evidence map›Paper›PMID 11160389›Full record

ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2001

C-terminal interaction is essential for surface trafficking but not for heteromeric assembly of GABA(b) receptors.

A Pagano, G Rovelli, J Mosbacher, T Lohmann, B Duthey, D Stauffer, D Ristig, V Schuler, I Meigel, C Lampert and 9 more

Abstract read
In one paragraph

Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 109 papers.

0numbers the graph read from it
0cells of the map it votes in
109citing papers in PubMed
–field-weighted citation impact
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

109 citing papers in PubMed.

  1. Article
  2. Article
  3. GABA-independent activation of GABANature communications · 2025
    Article
  4. Structural Basis of GABAAdvanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
  5. Article
  6. Monoallelic de novoScience advances · 2024
    Article
  7. Review
  8. Control of CCR5 Cell-Surface Targeting by the PRAF2 Gatekeeper.International journal of molecular sciences · 2023
    Article
  9. Article
  10. Article
  11. Structural Basis of GABACurrent topics in behavioral neurosciences · 2022
    Review
  12. Review
  13. Review
  14. GABACurrent topics in behavioral neurosciences · 2022
    Review
  15. Mechanisms and Regulation of Neuronal GABACurrent topics in behavioral neurosciences · 2022
    Review
  16. Ectopic activation of GABANature ecology & evolution · 2021
    Article
  17. Interface Prediction for GPCR Oligomerization Between Transmembrane Helices.Methods in molecular biology (Clifton, N.J.) · 2021
    Article
  18. Review
  19. Article
  20. Article

49 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

19 authors.

A PaganoNovartis Pharma AG, Therapeutic Area Nervous System, CH-4002 Basle, Switzerland.
G Rovelli
J Mosbacher
T Lohmann
B Duthey
D Stauffer
D Ristig
V Schuler
I Meigel
C Lampert
T Stein
L Prezeau
J Blahos
J Pin
W Froestl
R Kuhn
J Heid
K Kaupmann
B Bettler

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Assembly of fully functional GABA(B) receptors requires heteromerization of the GABA(B(1)) and GABA(B(2)) subunits. It is thought that GABA(B(1)) and GABA(B(2)) undergo coiled-coil dimerization in their cytoplasmic C termini and that assembly is necessary to overcome GABA(B(1)) retention in the endoplasmatic reticulum (ER). We investigated the mechanism underlying GABA(B(1)) trafficking to the cell surface. We identified a signal, RSRR, proximal to the coiled-coil domain of GABA(B(1)) that when deleted or mutagenized allows for surface delivery in the absence of GABA(B(2)). A similar motif, RXR, was recently shown to function as an ER retention/retrieval (ERR/R) signal in K(ATP) channels, demonstrating that G-protein-coupled receptors (GPCRs) and ion channels use common mechanisms to control surface trafficking. A C-terminal fragment of GABA(B(2)) is able to mask the RSRR signal and to direct the GABA(B(1)) monomer to the cell surface, where it is functionally inert. This indicates that in the heteromer, GABA(B(2)) participates in coupling to the G-protein. Mutagenesis of the C-terminal coiled-coil domains in GABA(B(1)) and GABA(B(2)) supports the possibility that their interaction is involved in shielding the ERR/R signal. However, assembly of heteromeric GABA(B) receptors is possible in the absence of the C-terminal domains, indicating that coiled-coil interaction is not necessary for function. Rather than guaranteeing heterodimerization, as previously assumed, the coiled-coil structure appears to be important for export of the receptor complex from the secretory apparatus.

Indexed as

Amino Acid MotifsCalciumCell LineCell MembraneDimerizationEndoplasmic ReticulumGTP-Binding ProteinsHumansImmunohistochemistryKidneyMutagenesis, Site-DirectedNeuronsPhotoaffinity LabelsProtein BindingProtein Structure, TertiaryProtein SubunitsCalciumGTP-Binding ProteinsPhotoaffinity LabelsProtein SubunitsReceptors, GABA-BReceptors, Metabotropic Glutamate

Identifiers

PMID11160389
PMCPMC6762227

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.