ArticleThe Journal of biological chemistry2017
Dimerization of the transmembrane domain of amyloid precursor protein is determined by residues around the γ-secretase cleavage sites.
Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed.
- Familial Alzheimer's disease mutations in amyloid precursor protein impair calcineurin signaling to NMDA receptors.The Journal of biological chemistry · 2025Article
- Cholesterol and Lipid Rafts in the Biogenesis of Amyloid-β Protein and Alzheimer's Disease.Annual review of biophysics · 2024Review
- Cholesterol-dependent amyloid β production: space for multifarious interactions between amyloid precursor protein, secretases, and cholesterol.Cell & bioscience · 2023Review
- Formation of extramembraneProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Structural Determinant of β-Amyloid Formation: From Transmembrane Protein Dimerization to β-Amyloid Aggregates.Biomedicines · 2022Review
- NanoBRET in C. elegans illuminates functional receptor interactions in real time.BMC molecular and cell biology · 2022Article
- Anti-Parallel β-Hairpin Structure in Soluble Aβ Oligomers of Aβ40-Dutch and Aβ40-Iowa.International journal of molecular sciences · 2021Article
- Bicelles Rich in both Sphingolipids and Cholesterol and Their Use in Studies of Membrane Proteins.Journal of the American Chemical Society · 2020Article
- Regulation of the alternative β-secretase meprin β by ADAM-mediated shedding.Cellular and molecular life sciences : CMLS · 2019Review
- Reciprocal modulation between amyloid precursor protein and synaptic membrane cholesterol revealed by live cell imaging.Neurobiology of disease · 2019Article
- The vexing complexity of the amyloidogenic pathway.Protein science : a publication of the Protein Society · 2019Review
- Emerging Diversity in Lipid-Protein Interactions.Chemical reviews · 2019Review
- Influence of the familial Alzheimer's disease-associated T43I mutation on the transmembrane structure and γ-secretase processing of the C99 peptide.The Journal of biological chemistry · 2019Article
- Structure of APP-C99Biochimica et biophysica acta. Biomembranes · 2018Article
- Article
- Dysregulation of Neuronal Iron Homeostasis as an Alternative Unifying Effect of Mutations Causing Familial Alzheimer's Disease.Frontiers in neuroscience · 2018Article
- Streptavidin Bead Pulldown Assay to Determine Protein Homooligomerization.Bio-protocol · 2017Article
- γ-Secretase Epsilon-cleavage Assay.Bio-protocol · 2017Article
- Detection of Membrane Protein Interactions by Cell-based Tango Assays.Bio-protocol · 2017Article
- The C99 domain of the amyloid precursor protein resides in the disordered membrane phase.The Journal of biological chemistryArticle
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Authors and funding
6 authors.
Funding
Abstract
One of the hallmarks of Alzheimer's disease is the formation of extracellular amyloid plaques that consist mainly of abnormally aggregated forms of amyloid β (Aβ) peptides. These peptides are generated by γ-secretase-catalyzed cleavage of a dimeric membrane-bound C-terminal fragment (C99) of the amyloid precursor protein. Although C99 homodimerization has been linked to Aβ production and changes in the aggregation-determining Aβ42/Aβ40 ratio, the motif through which C99 dimerizes has remained controversial. Here, we have used two independent assays to gain insight into C99 homodimerization in the context of the membrane of live cells: bioluminescence resonance energy transfer and Tango membrane protein-protein interaction assays, which were further confirmed by traditional pull-down assays. Our results indicate a four-amino acid region within the C99 transmembrane helix (
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