Evidence map›Paper›PMID 15470141›Full record

ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2004

Ral and phospholipase D2-dependent pathway for constitutive metabotropic glutamate receptor endocytosis.

Moshmi Bhattacharya, Andy V Babwah, Christina Godin, Pieter H Anborgh, Lianne B Dale, Michael O Poulter, Stephen S G Ferguson

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
2.6field-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

33 citing papers in PubMed, 92 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Review
  5. Article
  6. Review
  7. Article
  8. Metabotropic glutamate receptor trafficking.Molecular and cellular neurosciences · 2018
    Review
  9. Article
  10. Review
  11. Phosphatidic acid and neurotransmission.Advances in biological regulation · 2017
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Review
  20. 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

7 authors at 3 institutions in 1 country.

Moshmi BhattacharyaCell Biology Research Group, Robarts Research Institute, London, Ontario, Canada N6A 5K8.
Andy V Babwah
Christina Godin
Pieter H Anborgh
Lianne B Dale
Michael O Poulter
Stephen S G Ferguson
Robarts Clinical Trials · CACarleton University · CAWestern University · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

G-protein-coupled receptors play a central role in the regulation of neuronal cell communication. Class 1 metabotropic glutamate receptors (mGluRs) mGluR1a and mGluR5a, which are coupled with the hydrolysis of phosphoinositides, are essential for modulating excitatory neurotransmission at glutamatergic synapses. These receptors are constitutively internalized in heterologous cell cultures, neuronal cultures, and intact neuronal tissues. We show here that the small GTP-binding protein Ral, its guanine nucleotide exchange factor RalGDS (Ral GDP dissociation stimulator), and phospholipase D2 (PLD2) are constitutively associated with class 1 mGluRs and regulate constitutive mGluR endocytosis. Moreover, both Ral and PLD2 are colocalized with mGluRs in endocytic vesicles in both human embryonic kidney 293 (HEK 293) cells and neurons. Ral and PLD2 activity is required for the internalization of class 1 mGluRs but is not required for the internalization of the beta2-adrenergic receptor. Constitutive class 1 mGluR internalization is not dependent on the downstream Ral effector proteins Ral-binding protein 1 and PLD1 or either ADP-ribosylation factors ARF1 or ARF6. The treatment of HEK 293 cells and neurons with small interfering RNA both downregulates PLD2 expression and blocks mGluR1a and mGluR5a endocytosis. The constitutive internalization of mGluR1a and mGluR5a is also attenuated by the treatment of cells with 1-butanol to prevent PLD2-mediated phosphatidic acid formation. We propose that the formation of a mGluR-scaffolded RalGDS/Ral/PLD2 protein complex provides a novel alternative mechanism to beta-arrestins for the constitutive endocytosis of class 1 mGluRs.

Indexed as

EndocytosisAnimalsCell LineCells, CulturedHumansNeuronsPhospholipase Dral GTP-Binding ProteinsRatsReceptor, Metabotropic Glutamate 5Receptors, Metabotropic GlutamateSignal TransductionGRM5 protein, humanmetabotropic glutamate receptor type 1Phospholipase Dphospholipase D2ral GTP-Binding ProteinsReceptor, Metabotropic Glutamate 5Receptors, Metabotropic Glutamate

Identifiers

PMID15470141
PMCPMC6729950
OpenAlexW2159214937

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.