Evidence map›Paper›PMID 27035969›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2016

CRF binding protein facilitates the presence of CRF type 2α receptor on the cell surface.

Paula G Slater, Cledi A Cerda, Luis A Pereira, María E Andrés, Katia Gysling

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
3.8field-weighted citation impact, top 6% 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

26 citing papers in PubMed, 52 citations in OpenAlex.

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  11. Urocortins in the mammalian endocrine system.Acta veterinaria Scandinavica · 2019
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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 1 institution in 1 country.

Paula G SlaterDepartment of Cellular and Molecular Biology, Faculty of Biological Sciences, Pontificia Universidad Católica de Chile, 8331150 Santiago, Chile.
Cledi A CerdaDepartment of Cellular and Molecular Biology, Faculty of Biological Sciences, Pontificia Universidad Católica de Chile, 8331150 Santiago, Chile.
Luis A PereiraDepartment of Cellular and Molecular Biology, Faculty of Biological Sciences, Pontificia Universidad Católica de Chile, 8331150 Santiago, Chile.
María E AndrésDepartment of Cellular and Molecular Biology, Faculty of Biological Sciences, Pontificia Universidad Católica de Chile, 8331150 Santiago, Chile.
Katia GyslingDepartment of Cellular and Molecular Biology, Faculty of Biological Sciences, Pontificia Universidad Católica de Chile, 8331150 Santiago, Chile kgysling@bio.puc.cl.
Pontificia Universidad Católica de Chile · CL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Corticotropin releasing factor binding protein (CRF-BP) was originally recognized as CRF sequestering protein. However, its differential subcellular localization in different brain nuclei suggests that CRF-BP may have additional functions. There is evidence that CRF-BP potentiates CRF and urocortin 1 actions through CRF type 2 receptors (CRF2R). CRF2R is a G protein-coupled receptor (GPCR) that is found mainly intracellularly as most GPCRs. The access of GPCRs to the cell surface is tightly regulated by escort proteins. We hypothesized that CRF-BP binds to CRF2R, exerting an escort protein role. We analyzed the colocalization of CRF-BP and CRF2R in cultured rat mesencephalic neurons, and the localization and interaction of heterologous expressed CRF-BP and CRF2αR in yeast, human embryonic kidney 293, and rat pheochromocytoma 12 cells. Our results showed that CRF-BP and CRF2R naturally colocalize in the neurites of cultured mesencephalic neurons. Heterologous expression of each protein showed that CRF-BP was localized mainly in secretory granules and CRF2αR in the endoplasmic reticulum. In contrast, CRF-BP and CRF2αR colocalized when both proteins are coexpressed. Here we show that CRF-BP physically interacts with the CRF2αR but not the CRF2βR isoform, increasing CRF2αR on the cell surface. Thus, CRF-BP emerges as a GPCR escort protein increasing the understanding of GPCR trafficking.

Indexed as

AnimalsCarrier ProteinsCell MembraneFemaleHEK293 CellsHumansPC12 CellsPregnancyRatsRats, Sprague-DawleyReceptors, Corticotropin-Releasing HormoneSubcellular FractionsCarrier Proteinscorticotropin releasing factor-binding proteinCRF receptor type 2Receptors, Corticotropin-Releasing Hormoneaccessory proteinCRHescort proteinprotein interactions

Identifiers

PMID27035969
PMCPMC4839449
OpenAlexW2333356966

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.