ArticlePrion
Identification of PrP sequences essential for the interaction between the PrP polymers and Aβ peptide in a yeast-based assay.
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Who cites it
17 citing papers in PubMed, 26 citations in OpenAlex.
- Article
- Amyloid fibrils of the myelin basic protein are an integral component of myelin in the vertebrate brain.Scientific reports · 2025Article
- Prion-like Properties of Short Isoforms of Human Chromatin Modifier PHC3.International journal of molecular sciences · 2025Article
- The Aβ42 Peptide and IAPP Physically Interact in a Yeast-Based Assay.International journal of molecular sciences · 2023Article
- Alzheimer's Disease: Significant Benefit from the Yeast-Based Models.International journal of molecular sciences · 2023Review
- Regulation by Different Types of Chaperones of Amyloid Transformation of Proteins Involved in the Development of Neurodegenerative Diseases.International journal of molecular sciences · 2022Review
- Quantitative interrogation of protein co-aggregation using multi-color fluorogenic protein aggregation sensors.Chemical science · 2021Article
- Recent Advancements in Electrochemical Biosensors for Alzheimer's Disease Biomarkers Detection.Current medicinal chemistry · 2021Review
- Application of yeast to studying amyloid and prion diseases.Advances in genetics · 2020Review
- Protein Misfolding during Pregnancy: New Approaches to Preeclampsia Diagnostics.International journal of molecular sciences · 2019Review
- FRET Microscopy in Yeast.Biosensors · 2019Review
- Yeast Models for Amyloids and Prions: Environmental Modulation and Drug Discovery.Molecules (Basel, Switzerland) · 2019Review
- An aggregation-prone mutant of eIF3a forms reversible assemblies escaping spatial control in exponentially growing yeast cells.Current genetics · 2019Article
- Protein Co-Aggregation Related to Amyloids: Methods of Investigation, Diversity, and Classification.International journal of molecular sciences · 2018Review
- Mammalian amyloidogenic proteins promote prion nucleation in yeast.The Journal of biological chemistry · 2018Article
- Strain conformation controls the specificity of cross-species prion transmission in the yeast model.Prion · 2016Article
- Proteomic screening for amyloid proteins.PloS one · 2014Article
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
Alzheimer disease is associated with the accumulation of oligomeric amyloid β peptide (Aβ), accompanied by synaptic dysfunction and neuronal death. Polymeric form of prion protein (PrP), PrP(Sc), is implicated in transmissible spongiform encephalopathies (TSEs). Recently, it was shown that the monomeric cellular form of PrP (PrP(C)), located on the neuron surface, binds Aβ oligomers (and possibly other β-rich conformers) via the PrP(23-27) and PrP(90-110) segments, acting as Aβ receptor. On the other hand, PrP(Sc) polymers efficiently bind to Aβ monomers and accelerate their oligomerization. To identify specific PrP sequences that are essential for the interaction between PrP polymers and Aβ peptide, we have co-expressed Aβ and PrP (or its shortened derivatives), fused to different fluorophores, in the yeast cell. Our data show that the 90-110 and 28-89 regions of PrP control the binding of proteinase-resistant PrP polymers to the Aβ peptide, whereas the 23-27 segment of PrP is dispensable for this interaction. This indicates that the set of PrP fragments involved in the interaction with Aβ depends on PrP conformational state.
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Registered trials
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.