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Diversity of Amyloid Motifs in NLR Signaling in Fungi

Amyloid folds not only represent the underlying cause of a large class of human diseases but also display a variety of functional roles both in prokaryote and eukaryote organisms. Among these roles is a recently-described activity in signal transduction cascades functioning in host defense and progr...

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Autores principales: Loquet, Antoine, Saupe, Sven J.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5485727/
https://www.ncbi.nlm.nih.gov/pubmed/28406433
http://dx.doi.org/10.3390/biom7020038
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author Loquet, Antoine
Saupe, Sven J.
author_facet Loquet, Antoine
Saupe, Sven J.
author_sort Loquet, Antoine
collection PubMed
description Amyloid folds not only represent the underlying cause of a large class of human diseases but also display a variety of functional roles both in prokaryote and eukaryote organisms. Among these roles is a recently-described activity in signal transduction cascades functioning in host defense and programmed cell death and involving Nod-like receptors (NLRs). In different fungal species, prion amyloid folds convey activation signals from a receptor protein to an effector domain by an amyloid templating and propagation mechanism. The discovery of these amyloid signaling motifs derives from the study of [Het-s], a fungal prion of the species Podospora anserina. These signaling pathways are typically composed of two basic components encoded by adjacent genes, the NLR receptor bearing an amyloid motif at the N-terminal end and a cell death execution protein with a HeLo pore-forming domain bearing a C-terminal amyloid motif. Activation of the NLR receptor allows for amyloid folding of the N-terminal amyloid motifs which then template trans-conformation of the homologous motif in the cell death execution protein. A variety of such motifs, which differ by their sequence signature, have been described in fungi. Among them, the PP-motif bears resemblance with the RHIM amyloid motif involved in the necroptosis pathway in mammals suggesting an evolutionary conservation of amyloid signaling from fungi to mammals.
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spelling pubmed-54857272017-06-29 Diversity of Amyloid Motifs in NLR Signaling in Fungi Loquet, Antoine Saupe, Sven J. Biomolecules Review Amyloid folds not only represent the underlying cause of a large class of human diseases but also display a variety of functional roles both in prokaryote and eukaryote organisms. Among these roles is a recently-described activity in signal transduction cascades functioning in host defense and programmed cell death and involving Nod-like receptors (NLRs). In different fungal species, prion amyloid folds convey activation signals from a receptor protein to an effector domain by an amyloid templating and propagation mechanism. The discovery of these amyloid signaling motifs derives from the study of [Het-s], a fungal prion of the species Podospora anserina. These signaling pathways are typically composed of two basic components encoded by adjacent genes, the NLR receptor bearing an amyloid motif at the N-terminal end and a cell death execution protein with a HeLo pore-forming domain bearing a C-terminal amyloid motif. Activation of the NLR receptor allows for amyloid folding of the N-terminal amyloid motifs which then template trans-conformation of the homologous motif in the cell death execution protein. A variety of such motifs, which differ by their sequence signature, have been described in fungi. Among them, the PP-motif bears resemblance with the RHIM amyloid motif involved in the necroptosis pathway in mammals suggesting an evolutionary conservation of amyloid signaling from fungi to mammals. MDPI 2017-04-13 /pmc/articles/PMC5485727/ /pubmed/28406433 http://dx.doi.org/10.3390/biom7020038 Text en © 2017 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Loquet, Antoine
Saupe, Sven J.
Diversity of Amyloid Motifs in NLR Signaling in Fungi
title Diversity of Amyloid Motifs in NLR Signaling in Fungi
title_full Diversity of Amyloid Motifs in NLR Signaling in Fungi
title_fullStr Diversity of Amyloid Motifs in NLR Signaling in Fungi
title_full_unstemmed Diversity of Amyloid Motifs in NLR Signaling in Fungi
title_short Diversity of Amyloid Motifs in NLR Signaling in Fungi
title_sort diversity of amyloid motifs in nlr signaling in fungi
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5485727/
https://www.ncbi.nlm.nih.gov/pubmed/28406433
http://dx.doi.org/10.3390/biom7020038
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