Evidence map›Paper›PMID 25380825›Full record

ArticleJournal of cell science2015

EFR3s are palmitoylated plasma membrane proteins that control responsiveness to G-protein-coupled receptors.

Naveen Bojjireddy, Maria Luisa Guzman-Hernandez, Nathalie Renée Reinhard, Marko Jovic, Tamas Balla

Open access · bronzeAbstract read
In one paragraph

Article in Journal of cell science, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
1.0field-weighted citation impact, top 24% 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

37 citing papers in PubMed, 48 citations in OpenAlex.

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  13. Molecular basis for plasma membrane recruitment of PI4KA by EFR3.bioRxiv : the preprint server for biology · 2024
    Article
  14. Efr3b is essential for social recognition by modulating the excitability of CA2 pyramidal neurons.Proceedings of the National Academy of Sciences of the United States of America · 2024
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  15. Article
  16. Review
  17. EFR3A: a new raft domain organizing protein?Cellular & molecular biology letters · 2023
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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

5 authors at 3 institutions in 2 countries.

Naveen BojjireddySection on Molecular Signal Transduction, Program for Developmental Neuroscience, Eunice Kennedy Shriver NICHD, National Institutes of Health, Bethesda, MD 20892, USA.
Maria Luisa Guzman-HernandezSection on Molecular Signal Transduction, Program for Developmental Neuroscience, Eunice Kennedy Shriver NICHD, National Institutes of Health, Bethesda, MD 20892, USA.
Nathalie Renée ReinhardSwammerdam Institute for Life Sciences, University of Amsterdam, 1012 WX Amsterdam, The Netherlands.
Marko JovicSection on Molecular Signal Transduction, Program for Developmental Neuroscience, Eunice Kennedy Shriver NICHD, National Institutes of Health, Bethesda, MD 20892, USA.
Tamas BallaSection on Molecular Signal Transduction, Program for Developmental Neuroscience, Eunice Kennedy Shriver NICHD, National Institutes of Health, Bethesda, MD 20892, USA ballat@mail.nih.gov.
Eunice Kennedy Shriver National Institute of Child Health and Human Development · USNational Institutes of Health · USNetherlands Institute for Neuroscience · NL

Funding

Intramural NIH HHS
6 · The paper itself

Abstract

The yeast Efr3p protein is a main regulator of the Stt4p phosphatidylinositol 4-kinase at contact sites between the endoplasmic reticulum and the plasma membrane. A mutation in its fly homologue Rbo, leads to diminished light responses in the eye attributed to progressively impaired PLC signaling. Here, we find that Efr3s plays a role in maintaining responsiveness to the type-I angiotensin II (AngII) receptors. siRNA-mediated depletion of EFR3A and EFR3B impaired the sustained phase of cytosolic Ca(2+) response to high concentration of AngII in HEK293 cells that express wild type but not truncated AGTR1 (AT1a receptor), missing the phosphorylation sites. Efr3 depletion had minimal effect on the recovery of plasma membrane phosphoinositides during stimulation, and AT1 receptors still underwent ligand-induced internalization. A higher level of basal receptor phosphorylation and a larger response was observed after stimulation. Moreover, Gq activation more rapidly desensitized after AngII stimulation in Efr3 downregulated cells. A similar but less pronounced effect of EFR3 depletion was observed on the desensitization of the cAMP response after stimulation with isoproterenol. These data suggest that mammalian Efr3s contribute to the control of the phosphorylation state and, hence, desensitization of AT1a receptors, and could affect responsiveness of G-protein-coupled receptors in higher eukaryotes.

Indexed as

Adrenergic beta-AgonistsCyclic AMPHEK293 CellsHumansIsoproterenolLipoylationPhosphorylationReceptor, Angiotensin, Type 1Second Messenger SystemsAdrenergic beta-AgonistsAGTR1 protein, humanCyclic AMPIsoproterenolReceptor, Angiotensin, Type 1Angiotensin IIEFR3GPCRPhosphoinositidePI 4-kinaseReceptor desensitization

Identifiers

PMID25380825
PMCPMC4282049
OpenAlexW2120785003

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.