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Detecting Amyloid-β Accumulation via Immunofluorescent Staining in a Mouse Model of Alzheimer's Disease
Published on: April 19, 2021
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The expanding scope of amyloid signalling
1Institut de Biochimie et de Génétique Cellulaire (CNRS UMR 5095, Université de Bordeaux) , France.
Prion
|February 12, 2021
Summary
Functional amyloids form supramolecular complexes in cell death pathways across species. Research reveals conserved folds and links fungal [Het-s] prions to mammalian RHIM domains in amyloid signaling.
Area of Science:
- Biochemistry
- Molecular Biology
- Cell Biology
Background:
- Supramolecular complex formation is key in immune and cell-death signaling pathways.
- Functional amyloid motifs are involved in the assembly of some signalosomes.
- Fungal prions like [Het-s] provide early insights into these systems.
Purpose of the Study:
- To provide an integrated view of amyloid signaling in microbes, drawing parallels with animal systems.
- To analyze recent studies on functional amyloids in microbial signaling.
- To explore conserved folds, seeding mechanisms, and evolutionary links in amyloid-based signaling.
Main Methods:
- Review and commentary on three recent studies concerning amyloid signaling in microbes.
- Comparative analysis of fungal amyloid motifs and mammalian RHIM domains.
- Exploration of Nod-like receptor-based amyloid signalosomes in prokaryotes.
Main Results:
- Demonstrated conserved folds in functional amyloids and elucidated the structural basis of seeding.
- Established a relationship between fungal amyloid motifs and mammalian RIP homotypic interaction motifs (RHIM).
- Expanded the understanding of amyloid signalosomes to include prokaryotic systems.
Conclusions:
- Functional amyloids play a conserved role in diverse signaling pathways from fungi to mammals.
- The structural and mechanistic insights into amyloid formation are crucial for understanding cell death and immunity.
- Amyloid-based signaling represents an ancient mechanism with broad implications across prokaryotes and eukaryotes.
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