ArticleScientific reports2015
Theme and variations: evolutionary diversification of the HET-s functional amyloid motif.
Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 38 citations in OpenAlex.
- Functional amyloids as molecular switches: emerging roles in diverse signalling pathways.Biochemical Society transactions · 2026Review
- A functional amyloid scaffold shapes insect egg coats.bioRxiv : the preprint server for biology · 2026Article
- Regulated cell death in fungi from a comparative immunology perspective.Cell death and differentiation · 2026Review
- Harnessing deep learning for proteome-scale detection of amyloid signaling motifs.Bioinformatics (Oxford, England) · 2025Article
- Experimental methods for studying amyloid cross-interactions.Protein science : a publication of the Protein Society · 2025Review
- Molecular characterization of the N-terminal half of TasA during amyloid-like assembly and its contribution to Bacillus subtilis biofilm formation.NPJ biofilms and microbiomes · 2023Article
- Exploring a diverse world of effector domains and amyloid signaling motifs in fungal NLR proteins.PLoS computational biology · 2022Article
- Allorecognition genes drive reproductive isolation in Podospora anserina.Nature ecology & evolution · 2022Article
- The expanding scope of amyloid signalling.Prion · 2021Article
- Searching for universal model of amyloid signaling motifs using probabilistic context-free grammars.BMC bioinformatics · 2021Article
- Article
- Structural and molecular basis of cross-seeding barriers in amyloids.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Structures of Pathological and Functional Amyloids and Prions, a Solid-State NMR Perspective.Frontiers in molecular neuroscience · 2021Review
- RPW8/HR repeats control NLR activation in Arabidopsis thaliana.PLoS genetics · 2019Article
- Microbial functional amyloids serve diverse purposes for structure, adhesion and defence.Biophysical reviews · 2019Review
- Estimating probabilistic context-free grammars for proteins using contact map constraints.PeerJ · 2019Article
- Diversity of Amyloid Motifs in NLR Signaling in Fungi.Biomolecules · 2017Review
- Article
- Identification of a novel cell death-inducing domain reveals that fungal amyloid-controlled programmed cell death is related to necroptosis.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Proline and lysine residues provide modulatory switches in amyloid formation: Insights from prion protein.Prion · 2016Article
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Authors and funding
3 authors at 2 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In mammals and fungi, Nod-like receptors (NLR) activate downstream cell death execution proteins by a prion-like mechanism. In Podospora anserina, the NWD2 NLR activates the HET-S Helo-domain pore-forming protein by converting its prion-forming domain into a characteristic β-solenoid amyloid fold. The amyloid forming region of HET-S/s comprises two repetitions of a 21 amino acid motif. Herein, we systematically analyze the sequences of C-terminal regions of fungal HeLo and HeLo-like domain proteins to identify HET-s-related amyloid motifs (HRAM). We now identify four novel HRAM subfamilies in addition to the canonical HET-S/s subfamily. These novel motifs share the pseudo-repeat structure of HET-S/s and a specific pattern of distribution of hydrophobic and polar residues. Sequence co-variance analyses predict parallel in-register β-stacking of the two repeats and residue-residue interactions compatible with the β-solenoid fold. As described for HET-S, most genes encoding the HeLo proteins are adjacent to genes encoding NLRs also displaying HRAMs. The motifs of the NLRs are similar to those of their cognate HeLo-domain protein, indicating concerted evolution between repeats. This study shows that HET-s-related amyloid motifs are more common than anticipated and that they have diversified into discrete subfamilies that apparently share a common overall fold.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.