Evidence map›Paper›PMID 30729188›Full record

ArticleCommunications biology2019

Crystal structures of human lysosomal EPDR1 reveal homology with the superfamily of bacterial lipoprotein transporters.

Yong Wei, Zi Jian Xiong, Jun Li, Chunxia Zou, Christopher W Cairo, John S Klassen, Gilbert G Privé

Open access · greenAbstract read
In one paragraph

Article in Communications biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
–field-weighted citation impact
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

18 citing papers in PubMed, 19 citations in OpenAlex.

  1. Expression and significance of ependymin-related protein 1 and neuregulin 4 in the serum of patients with polycystic ovary syndrome.International journal of gynaecology and obstetrics: the official organ of the International Federation of Gynaecology and Obstetrics · 2026
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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

7 authors at 2 institutions in 1 country.

Yong Wei1Princess Margaret Cancer Centre, Toronto, M5G 1L7 ON Canada.ORCID 0000-0002-3314-118X
Zi Jian Xiong2Department of Biochemistry, University of Toronto, Toronto, M5S 1A8 ON Canada.ORCID 0000-0002-7170-0472
Jun Li3Alberta Glycomics Centre and Department of Chemistry, University of Alberta, Edmonton, T6G 2G2 AB Canada.
Chunxia Zou3Alberta Glycomics Centre and Department of Chemistry, University of Alberta, Edmonton, T6G 2G2 AB Canada.
Christopher W Cairo3Alberta Glycomics Centre and Department of Chemistry, University of Alberta, Edmonton, T6G 2G2 AB Canada.ORCID 0000-0003-3363-8708
John S Klassen3Alberta Glycomics Centre and Department of Chemistry, University of Alberta, Edmonton, T6G 2G2 AB Canada.
Gilbert G Privé1Princess Margaret Cancer Centre, Toronto, M5G 1L7 ON Canada.ORCID 0000-0002-0712-4319
Princess Margaret Cancer Centre · CAUniversity of Toronto · CA

Funding

Overall (pp. 40-62)P41GM103485 · NIGMS · CORNELL UNIVERSITY · PI CERIONE, RICHARD A. · 2012 to 2018
$15.5M
NIGMS NIH HHS P41 GM103485
6 · The paper itself

Abstract

EPDR1, a member of the ependymin-related protein family, is a relatively uncharacterized protein found in the lysosomes and secretomes of most vertebrates. Despite having roles in human disease and health, the molecular functions of EPDR1 remain unknown. Here, we present crystal structures of human EPDR1 and reveal that the protein adopts a fold previously seen only in bacterial proteins related to the LolA lipoprotein transporter. EPDR1 forms a homodimer with an overall shape resembling a half-shell with two non-overlapping hydrophobic grooves on the flat side of the hemisphere. EPDR1 can interact with membranes that contain negatively charged lipids, including BMP and GM1, and we suggest that EPDR1 may function as a lysosomal activator protein or a lipid transporter. A phylogenetic analysis reveals that the fold is more widely distributed than previously suspected, with representatives identified in all branches of cellular life.

Indexed as

Amino Acid SequenceAnimalsBaculoviridaeBinding SitesCloning, MolecularCrystallography, X-RayEscherichia coliEscherichia coli ProteinsGene ExpressionG(M1) GangliosideHumansHydrophobic and Hydrophilic InteractionsIntercellular Signaling Peptides and ProteinsLysophospholipidsLysosomesModels, Molecularbis(monoacylglyceryl)phosphateEPDR1 protein, humanEscherichia coli ProteinsG(M1) GangliosideIntercellular Signaling Peptides and ProteinsLolA protein, E coliLysophospholipidsMonoglyceridesNeoplasm ProteinsNerve Tissue ProteinsPeriplasmic Binding ProteinsRecombinant Proteins

Identifiers

PMID30729188
PMCPMC6363788
OpenAlexW2914744085

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.