ArticleScientific reports2014
Evolutionary link between metazoan RHIM motif and prion-forming domain of fungal heterokaryon incompatibility factor HET-s/HET-s.
Article in Scientific reports, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed.
- Functional amyloids as molecular switches: emerging roles in diverse signalling pathways.Biochemical Society transactions · 2026Review
- 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
- Evolutionary and functional analyses reveal a role for the RHIM in tuning RIPK3 activity across vertebrates.eLife · 2025Article
- Bat RNA viruses employ viral RHIMs orchestrating species-specific cell death programs linked to Z-RNA sensing and ZBP1-RIPK3 signaling.iScience · 2024Article
- Proteomic Evidence for Amyloidogenic Cross-Seeding in Fibrinaloid Microclots.International journal of molecular sciences · 2024Article
- HSPA8 acts as an amyloidase to suppress necroptosis by inhibiting and reversing functional amyloid formation.Cell research · 2023Article
- Emergence of the fungal immune system.iScience · 2023Review
- Identification of New FG-Repeat Nucleoporins with Amyloid Properties.International journal of molecular sciences · 2023Article
- Exploring a diverse world of effector domains and amyloid signaling motifs in fungal NLR proteins.PLoS computational biology · 2022Article
- The role of RHIM in necroptosis.Biochemical Society transactions · 2022Article
- What makes functional amyloids work?Critical reviews in biochemistry and molecular biology · 2022Review
- Article
- The expanding scope of amyloid signalling.Prion · 2021Article
- Searching for universal model of amyloid signaling motifs using probabilistic context-free grammars.BMC bioinformatics · 2021Article
- The structure of a minimum amyloid fibril core formed by necroptosis-mediating RHIM of human RIPK3.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Article
- The Evolutionary Origins of Programmed Cell Death Signaling.Cold Spring Harbor perspectives in biology · 2020Review
- CK1α, CK1δ, and CK1ε are necrosome components which phosphorylate serine 227 of human RIPK3 to activate necroptosis.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Autophagy regulates inflammatory programmed cell death via turnover of RHIM-domain proteins.eLife · 2019Article
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4 authors.
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Abstract
The Rip homotypic interaction motif (RHIM) is a short, non-globular sequence stretch that mediates a key interaction of mammalian necroptosis signaling. In order to understand its unusual oligomerization properties, we set out to trace the evolutionary origins of the RHIM motif by identifying distantly related protein motifs that might employ the same binding mode. The RHIM motif was found to be related to the prion-forming domain of the HET-s protein, which oligomerizes by forming structurally well-characterized fibrils and is involved in fungal heterokaryon incompatibility. This evolutionary relationship explains the recently reported propensity of mammalian RHIM motifs to form amyloid fibrils, but suggests that these fibrils have a different structural architecture than currently assumed. These findings, together with numerous observations of RHIM-like motifs in immunity proteins from a wide range of species, provide insight to the modern innate immunity pathways in animals, plants and fungi.
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