Evidence map›Paper›PMID 30423289›Full record

ArticleNeuropharmacology2019

GPR37 and GPR37L1 differently interact with dopamine 2 receptors in live cells.

E Hertz, L Terenius, V Vukojević, P Svenningsson

Open access · hybridAbstract read
In one paragraph

Article in Neuropharmacology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.1field-weighted citation impact, top 22% 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

14 citing papers in PubMed, 23 citations in OpenAlex.

  1. FromCells · 2026
    Review
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  9. GM1 Is Cytoprotective in GPR37-Expressing Cells and Downregulates Signaling.International journal of molecular sciences · 2021
    Article
  10. Article
  11. GPR37 is processed in the N-terminal ectodomain by ADAM10 and furin.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2021
    Article
  12. Ecto-GPR37: a potential biomarker for Parkinson's disease.Translational neurodegeneration · 2021
    Article
  13. Article
  14. 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

4 authors at 1 institution in 1 country.

E HertzDepartment of Clinical Neuroscience, Karolinska Institute, Stockholm, Sweden. Electronic address: ellen.hertz@ki.se.
L TereniusDepartment of Clinical Neuroscience, Karolinska Institute, Stockholm, Sweden.
V VukojevićDepartment of Clinical Neuroscience, Karolinska Institute, Stockholm, Sweden.
P SvenningssonDepartment of Clinical Neuroscience, Karolinska Institute, Stockholm, Sweden. Electronic address: per.svenningsson@ki.se.
Karolinska Institutet · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Receptor-receptor interactions are essential to fine tune receptor responses and new techniques enable closer characterization of the interactions between involved proteins directly in the plasma membrane. Fluorescence cross-correlation spectroscopy (FCCS), which analyses concurrent movement of bound molecules with single-molecule detection limit, was here used to, in live N2a cells, study interactions between the Parkinson's disease (PD) associated orphan receptor GPR37, its homologue GPR37L1, and the two splice variants of the dopamine 2 receptor (D2R). An interaction between GPR37 and both splice forms of D2R was detected. 4-phenylbutyrate (4-PBA), a neuroprotective chemical chaperone known to increase GPR37 expression at the cell surface, increased the fraction of interacting molecules. The interaction was also increased by pramipexole, a D2R agonist commonly used in the treatment of PD, indicating a possible clinically relevance. Cross-correlation, indicating interaction between GPR37L1 and the short isoform of D2R, was also detected. However, this interaction was not changed with 4-PBA or pramipexole treatment. Overall, these data provide further evidence that heteromeric GPR37-D2R exist and can be pharmacologically modulated, which is relevant for the treatment of PD. This article is part of the Special Issue entitled 'Receptor heteromers and their allosteric receptor-receptor interactions'.

Indexed as

AnimalsCell LineCell MembraneDopamine AgonistsHumansMicePramipexoleProtein BindingReceptors, Dopamine D2Receptors, G-Protein-CoupledDopamine AgonistsGPR37L1 protein, humanGPR37 receptor, humanPramipexoleReceptors, Dopamine D2Receptors, G-Protein-Coupled4-PBA fluorescence cross-correlation spectroscopyDopamine 2 receptorGPR37GPR37L1Pramipexole

Identifiers

PMID30423289
PMCPMC6599889
OpenAlexW2900181528

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.