Amyloid Signaling in Filamentous Fungi and Bacteria

Sven J Saupe1

  • 1Institut de Biochimie et de Génétique Cellulaire, UMR 5095 CNRS, Université de Bordeaux, 33077 Bordeaux CEDEX, France;

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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