The amyloid precursor protein is a conserved Wnt receptor.


Journal

eLife
ISSN: 2050-084X
Titre abrégé: Elife
Pays: England
ID NLM: 101579614

Informations de publication

Date de publication:
09 09 2021
Historique:
received: 09 04 2021
accepted: 01 09 2021
entrez: 13 9 2021
pubmed: 14 9 2021
medline: 28 10 2021
Statut: epublish

Résumé

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.

Identifiants

pubmed: 34515635
doi: 10.7554/eLife.69199
pii: 69199
pmc: PMC8437438
doi:
pii:

Substances chimiques

Amyloid beta-Protein Precursor 0
Appl protein, Drosophila 0
Drosophila Proteins 0
Membrane Proteins 0
Nerve Tissue Proteins 0
Receptors, Wnt 0
Vang protein, Drosophila 0

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Informations de copyright

© 2021, Liu et al.

Déclaration de conflit d'intérêts

TL, TZ, MN, LB, HR, AS, AC, IP, LF, BD, MP, BH No competing interests declared

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Auteurs

Tengyuan Liu (T)

Paris Brain Institute - Institut du Cerveau, Sorbonne Université, Inserm, CNRS, Hôpital Pitié-Salpêtrière, Paris, France.
Doctoral School of Biomedical Sciences, Leuven, Belgium.

Tingting Zhang (T)

Paris Brain Institute - Institut du Cerveau, Sorbonne Université, Inserm, CNRS, Hôpital Pitié-Salpêtrière, Paris, France.
Doctoral School of Biomedical Sciences, Leuven, Belgium.

Maya Nicolas (M)

Doctoral School of Biomedical Sciences, Leuven, Belgium.
Center for Brain and Disease, Leuven, Belgium.
Center for Human Genetics, University of Leuven School of Medicine, Leuven, Belgium.

Lydie Boussicault (L)

Paris Brain Institute - Institut du Cerveau, Sorbonne Université, Inserm, CNRS, Hôpital Pitié-Salpêtrière, Paris, France.

Heather Rice (H)

Center for Brain and Disease, Leuven, Belgium.
Center for Human Genetics, University of Leuven School of Medicine, Leuven, Belgium.

Alessia Soldano (A)

Center for Brain and Disease, Leuven, Belgium.
Center for Human Genetics, University of Leuven School of Medicine, Leuven, Belgium.

Annelies Claeys (A)

Center for Brain and Disease, Leuven, Belgium.
Center for Human Genetics, University of Leuven School of Medicine, Leuven, Belgium.

Iveta Petrova (I)

Laboratory of Developmental Neurobiology, Department of Molecular Cell Biology, Leiden University Medical Center, Leiden, Netherlands.

Lee Fradkin (L)

Laboratory of Developmental Neurobiology, Department of Molecular Cell Biology, Leiden University Medical Center, Leiden, Netherlands.

Bart De Strooper (B)

Center for Brain and Disease, Leuven, Belgium.
UK Dementia Research institute at University College London, London, United Kingdom.

Marie-Claude Potier (MC)

Paris Brain Institute - Institut du Cerveau, Sorbonne Université, Inserm, CNRS, Hôpital Pitié-Salpêtrière, Paris, France.

Bassem A Hassan (BA)

Paris Brain Institute - Institut du Cerveau, Sorbonne Université, Inserm, CNRS, Hôpital Pitié-Salpêtrière, Paris, France.

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