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Updated: Dec 14, 2025

Rapid Generation of Amyloid from Native Proteins In vitro
Published on: December 5, 2013
Amyloid Signaling in Filamentous Fungi and Bacteria
1Institut de Biochimie et de Génétique Cellulaire, UMR 5095 CNRS, Université de Bordeaux, 33077 Bordeaux CEDEX, France;
Abstract:
Amyloids are implicated in many protein misfolding diseases. Amyloid folds, however, also display a range of functional roles particularly in the microbial world. The templating ability of these folds endows them with specific properties allowing their self-propagation and protein-to-protein transmission in vivo. This property, the prion principle, is exploited by specific signaling pathways that use transmission of the amyloid fold as a way to convey information from a receptor to an effector protein. I describe here amyloid signaling pathways involving fungal nucleotide binding and oligomerization domain (NOD)-like receptors that were found to control nonself recognition and programmed cell death processes. Studies on these fungal amyloid signaling motifs stem from the characterization of the fungal [Het-s] prion protein and have led to the identification in fungi but also in multicellular bacteria of several distinct families of signaling motifs, one of which is related to RHIM [receptor-interacting protein (RIP) homotypic interaction motif], an amyloid motif regulating mammalian necroptosis.
Insights
Functional amyloids, like the fungal [Het-s] prion, act as signaling molecules. These amyloid structures transmit information via the prion principle, controlling processes like cell death and recognition.
Area of Science:
- Biochemistry
- Molecular Biology
- Microbiology
Background:
- Amyloids are known for their role in protein misfolding diseases.
- However, amyloid folds also possess functional roles, particularly in microbes.
- The prion principle describes the self-propagation and transmission of amyloid structures.
Purpose of the Study:
- To describe amyloid signaling pathways involving fungal nucleotide binding and oligomerization domain (NOD)-like receptors.
- To explore how these pathways control nonself recognition and programmed cell death.
- To identify novel signaling motifs related to known amyloid structures.
Main Methods:
- Characterization of the fungal [Het-s] prion protein.
- Identification of amyloid signaling motifs in fungi and bacteria.
- Comparison of fungal motifs with mammalian RHIM (receptor-interacting protein homotypic interaction motif) domains.
Main Results:
- Amyloid signaling pathways involving fungal NOD-like receptors control nonself recognition and programmed cell death.
- Several distinct families of signaling motifs were identified in fungi and multicellular bacteria.
- One identified motif is related to the RHIM domain, known to regulate mammalian necroptosis.
Conclusions:
- Functional amyloids serve as critical signaling molecules in microbial systems.
- The prion principle is exploited by signaling pathways to convey information.
- These findings reveal conserved amyloid signaling mechanisms across different organisms, including links to mammalian necroptosis.
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