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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...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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MDPI
2017
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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. |
format | Online Article Text |
id | pubmed-5485727 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
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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