Evidence map›Paper›PMID 34515635›Full record

ArticleeLife2021

The amyloid precursor protein is a conserved Wnt receptor.

Tengyuan Liu, Tingting Zhang, Maya Nicolas, Lydie Boussicault, Heather Rice, Alessia Soldano, Annelies Claeys, Iveta Petrova, Lee Fradkin, Bart De Strooper and 2 more

Open access · goldAbstract read
In one paragraph

Article in eLife, 2021. 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
3.2field-weighted citation impact, top 7% 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, 31 citations in OpenAlex.

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  4. Exploring huntington's disease from a neurodevelopmental perspective.International journal of biological sciences · 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

12 authors at 5 institutions in 5 countries.

Tengyuan LiuParis Brain Institute - Institut du Cerveau, Sorbonne Université, Inserm, CNRS, Hôpital Pitié-Salpêtrière, Paris, France.
Tingting ZhangParis Brain Institute - Institut du Cerveau, Sorbonne Université, Inserm, CNRS, Hôpital Pitié-Salpêtrière, Paris, France.
Maya NicolasDoctoral School of Biomedical Sciences, Leuven, Belgium.ORCID 0000-0002-7148-6357
Lydie BoussicaultParis Brain Institute - Institut du Cerveau, Sorbonne Université, Inserm, CNRS, Hôpital Pitié-Salpêtrière, Paris, France.
Heather RiceCenter for Brain and Disease, Leuven, Belgium.
Alessia SoldanoCenter for Brain and Disease, Leuven, Belgium.ORCID 0000-0002-3120-9929
Annelies ClaeysCenter for Brain and Disease, Leuven, Belgium.
Iveta PetrovaLaboratory of Developmental Neurobiology, Department of Molecular Cell Biology, Leiden University Medical Center, Leiden, Netherlands.
Lee FradkinLaboratory of Developmental Neurobiology, Department of Molecular Cell Biology, Leiden University Medical Center, Leiden, Netherlands.
Bart De StrooperCenter for Brain and Disease, Leuven, Belgium.ORCID 0000-0001-5455-5819
Marie-Claude PotierParis Brain Institute - Institut du Cerveau, Sorbonne Université, Inserm, CNRS, Hôpital Pitié-Salpêtrière, Paris, France.ORCID 0000-0003-2462-7150
Bassem A HassanParis Brain Institute - Institut du Cerveau, Sorbonne Université, Inserm, CNRS, Hôpital Pitié-Salpêtrière, Paris, France.ORCID 0000-0001-9533-4908
Centre National de la Recherche Scientifique · FRUniversity of Massachusetts Chan Medical School · USVIB-KU Leuven Center for Cancer Biology · BEVIB-VUB Center for Structural Biology · BEUK Dementia Research Institute · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Amyloid Precursor Protein (APP) and its homologues are transmembrane proteins required for various aspects of neuronal development and activity, whose molecular function is unknown. Specifically, it is unclear whether APP acts as a receptor, and if so what its ligand(s) may be. We show that APP binds the Wnt ligands Wnt3a and Wnt5a and that this binding regulates APP protein levels. Wnt3a binding promotes full-length APP (flAPP) recycling and stability. In contrast, Wnt5a promotes APP targeting to lysosomal compartments and reduces flAPP levels. A conserved Cysteine-Rich Domain (CRD) in the extracellular portion of APP is required for Wnt binding, and deletion of the CRD abrogates the effects of Wnts on flAPP levels and trafficking. Finally, loss of APP results in increased axonal and reduced dendritic growth of mouse embryonic primary cortical neurons. This phenotype can be cell-autonomously rescued by full length, but not CRD-deleted, APP and regulated by Wnt ligands in a CRD-dependent manner.

Indexed as

Amino Acid SequenceAmyloid beta-Protein PrecursorAnimalsBrainCells, CulturedCloning, MolecularDrosophila melanogasterDrosophila ProteinsGene DeletionGene Expression RegulationHumansMembrane ProteinsMiceMushroom BodiesNerve Tissue ProteinsNeuronsAmyloid beta-Protein PrecursorAppl protein, DrosophilaDrosophila ProteinsMembrane ProteinsNerve Tissue ProteinsReceptors, WntVang protein, Drosophilaalzheimer's diseaseamyloid precursor proteinbrain developmentcell biologyD. melanogasterDrosophilamouseneurosciencewnt

Identifiers

PMID34515635
PMCPMC8437438
OpenAlexW3199778280

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.