ArticleBiophysical journal2012
The amyloid precursor protein forms plasmalemmal clusters via its pathogenic amyloid-β domain.
Article in Biophysical journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Clustering hinders APP α-secretase processing in the plasma membrane.Biophysical journal · 2026Article
- Conformational and functional changes of the native neuropeptide somatostatin occur in the presence of copper and amyloid-β.Nature chemistry · 2022Article
- The transmembrane domain of the amyloid precursor protein is required for antiamyloidogenic processing by α-secretase ADAM10.The Journal of biological chemistry · 2022Article
- HPV caught in the tetraspanin web?Medical microbiology and immunology · 2020Article
- Packing Density of the Amyloid Precursor Protein in the Cell Membrane.Biophysical journal · 2018Article
- The packing density of a supramolecular membrane protein cluster is controlled by cytoplasmic interactions.eLife · 2017Article
- Forty years on: clathrin-coated pits continue to fascinate.Molecular biology of the cell · 2017Review
- No Evidence for Spontaneous Lipid Transfer at ER-PM Membrane Contact Sites.The Journal of membrane biology · 2016Article
- Surface Trafficking of APP and BACE in Live Cells.Traffic (Copenhagen, Denmark) · 2015Article
- Multi-protein assemblies underlie the mesoscale organization of the plasma membrane.Nature communications · 2014Article
- The extracellular δ-domain is essential for the formation of CD81 tetraspanin webs.Biophysical journal · 2014Article
- Article
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The amyloid precursor protein (APP) is a large, ubiquitous integral membrane protein with a small amyloid-β (Aβ) domain. In the human brain, endosomal processing of APP produces neurotoxic Aβ-peptides, which are involved in Alzheimer's disease. Here, we show that the Aβ sequence exerts a physiological function when still present in the unprocessed APP molecule. From the extracellular site, Aβ concentrates APP molecules into plasmalemmal membrane protein clusters. Moreover, Aβ stabilization of clusters is a prerequisite for their targeting to endocytic clathrin structures. Therefore, we conclude that the Aβ domain directly mediates a central step in APP trafficking, driving its own conversion into neurotoxic peptides.
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