Amyloid Signaling in Filamentous Fungi and Bacteria - CNRS - Centre national de la recherche scientifique
Journal Articles Annual Review of Microbiology Year : 2020

Amyloid Signaling in Filamentous Fungi and Bacteria

Sven J. Saupe

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.
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Dates and versions

hal-04833229 , version 1 (12-12-2024)

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Sven J. Saupe. Amyloid Signaling in Filamentous Fungi and Bacteria. Annual Review of Microbiology, 2020, 74 (1), pp.673--691. ⟨10.1146/annurev-micro-011320-013555⟩. ⟨hal-04833229⟩

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