Evidence map›Paper›PMID 25535841›Full record

ArticleeLife2014

Identification of PLXDC1 and PLXDC2 as the transmembrane receptors for the multifunctional factor PEDF.

Guo Cheng, Ming Zhong, Riki Kawaguchi, Miki Kassai, Muayyad Al-Ubaidi, Jun Deng, Mariam Ter-Stepanian, Hui Sun

Open access · goldAbstract read
In one paragraph

Article in eLife, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
1.7field-weighted citation impact, top 19% 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

51 citing papers in PubMed, 87 citations in OpenAlex.

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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

8 authors at 4 institutions in 1 country.

Guo ChengDepartment of Physiology, Howard Hughes Medical Institute, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, United States.
Ming ZhongDepartment of Physiology, Howard Hughes Medical Institute, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, United States.
Riki KawaguchiDepartment of Physiology, Howard Hughes Medical Institute, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, United States.
Miki KassaiDepartment of Physiology, Howard Hughes Medical Institute, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, United States.
Muayyad Al-UbaidiDepartment of Cell Biology, University of Oklahoma Health Sciences Center, Oklahoma City, United States.
Jun DengDepartment of Physiology, Howard Hughes Medical Institute, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, United States.
Mariam Ter-StepanianDepartment of Physiology, Howard Hughes Medical Institute, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, United States.
Hui SunDepartment of Physiology, Howard Hughes Medical Institute, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, United States.
Doheny Eye Institute · USHoward Hughes Medical Institute · USUniversity of California, Los Angeles · USUniversity of Oklahoma Health Sciences Center · US

Funding

Howard Hughes Medical Institute
6 · The paper itself

Abstract

Pigment Epithelium Derived Factor (PEDF) is a secreted factor that has broad biological activities. It was first identified as a neurotrophic factor and later as the most potent natural antiangiogenic factor, a stem cell niche factor, and an inhibitor of cancer cell growth. Numerous animal models demonstrated its therapeutic value in treating blinding diseases and diverse cancer types. A long-standing challenge is to reveal how PEDF acts on its target cells and the identities of the cell-surface receptors responsible for its activities. Here we report the identification of transmembrane proteins PLXDC1 and PLXDC2 as cell-surface receptors for PEDF. Using distinct cellular models, we demonstrate their cell type-specific receptor activities through loss of function and gain of function studies. Our experiments suggest that PEDF receptors form homooligomers under basal conditions, and PEDF dissociates the homooligomer to activate the receptors. Mutations in the intracellular domain can have profound effects on receptor activities.

Indexed as

Amino Acid SequenceBinding SitesEye ProteinsGene ExpressionHEK293 CellsHumansLigandsMolecular Sequence DataMutationNeoplasm ProteinsNerve Growth FactorsPigment Epithelium-Derived FactorProtein BindingProtein MultimerizationProtein Structure, TertiaryReceptors, Cell SurfaceEye ProteinsLigandsNeoplasm ProteinsNerve Growth FactorsPigment Epithelium-Derived FactorPLXDC1 protein, humanPLXDC2 protein, humanReceptors, Cell SurfaceRecombinant Fusion ProteinsSerpinsbiochemistrycell biologyhuman diseasemembrane receptorsnonesignal transduction

Identifiers

PMID25535841
PMCPMC4303762
OpenAlexW2112975677

What OpenQuestion holds

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LicenceCC BY
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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.