On the evolutionary trajectories of signal-transducing amyloids in fungi and beyond

Daskalov, Asen

doi:10.1080/19336896.2016.1228506

Cited by 7 publications

(7 citation statements)

References 34 publications

(56 reference statements)

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“…The widespread and diversity of amyloid prion domains underscores the evolutionary success of this class of signaling modules in fungi. Furthermore, we have uncovered a large variety of signaling amyloids with prion properties operating in analogous NLR-dependent signaling cascades ( Daskalov et al, 2015a ; Daskalov, 2016 ; Loquet and Saupe, 2017 ). In particular, the fungal PP motif ( Daskalov et al, 2016 ) shows sequence similarity to the RIP1/RIP3 necrosome in humans.…”

Section: Functional Prions Emerge As Trans -Kingdom Entitiesmentioning

confidence: 99%

Structures of Pathological and Functional Amyloids and Prions, a Solid-State NMR Perspective

Daskalov

Mammeri

Lends

et al. 2021

Front. Mol. Neurosci.

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Infectious proteins or prions are a remarkable class of pathogens, where pathogenicity and infectious state correspond to conformational transition of a protein fold. The conformational change translates into the formation by the protein of insoluble amyloid aggregates, associated in humans with various neurodegenerative disorders and systemic protein-deposition diseases. The prion principle, however, is not limited to pathogenicity. While pathological amyloids (and prions) emerge from protein misfolding, a class of functional amyloids has been defined, consisting of amyloid-forming domains under natural selection and with diverse biological roles. Although of great importance, prion amyloid structures remain challenging for conventional structural biology techniques. Solid-state nuclear magnetic resonance (SSNMR) has been preferentially used to investigate these insoluble, morphologically heterogeneous aggregates with poor crystallinity. SSNMR methods have yielded a wealth of knowledge regarding the fundamentals of prion biology and have helped to solve the structures of several prion and prion-like fibrils. Here, we will review pathological and functional amyloid structures and will discuss some of the obtained structural models. We will finish the review with a perspective on integrative approaches combining solid-state NMR, electron paramagnetic resonance and cryo-electron microscopy, which can complement and extend our toolkit to structurally explore various facets of prion biology.

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Section: Functional Prions Emerge As Trans -Kingdom Entitiesmentioning

confidence: 99%

Structures of Pathological and Functional Amyloids and Prions, a Solid-State NMR Perspective

Daskalov

Mammeri

Lends

et al. 2021

Front. Mol. Neurosci.

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“…To date, the immunoprecipitation method revealed that RIP1/RIP3 can compose a heteroamyloid [ 149 ], although the structural and functional relationships require further clarification. It is also worth noting that the RHIM motifs of RIP proteins are homologous to the prion domain of Het-s, a prion protein of the fungus Podospora anserina , that is also involved in the programmed mycelium destruction process, controlling the cytoplasmic incompatibility, a biologically advantageous process in fungi [ 154 , 155 ]. Proteins with similar domains and roles are also found in other fungi [ 156 ].…”

Section: Functional Amyloids In Mammalsmentioning

confidence: 99%

Functional Mammalian Amyloids and Amyloid-Like Proteins

Rubel

Fedotov

Grizel

et al. 2020

Life

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Amyloids are highly ordered fibrous cross-β protein aggregates that are notorious primarily because of association with a variety of incurable human and animal diseases (termed amyloidoses), including Alzheimer’s disease (AD), Parkinson’s disease (PD), type 2 diabetes (T2D), and prion diseases. Some amyloid-associated diseases, in particular T2D and AD, are widespread and affect hundreds of millions of people all over the world. However, recently it has become evident that many amyloids, termed “functional amyloids,” are involved in various activities that are beneficial to organisms. Functional amyloids were discovered in diverse taxa, ranging from bacteria to mammals. These amyloids are involved in vital biological functions such as long-term memory, storage of peptide hormones and scaffolding melanin polymerization in animals, substrate attachment, and biofilm formation in bacteria and fungi, etc. Thus, amyloids undoubtedly are playing important roles in biological and pathological processes. This review is focused on functional amyloids in mammals and summarizes approaches used for identifying new potentially amyloidogenic proteins and domains.

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“…This is reminiscent of the interaction between RPW8/HR proteins and the NLR protein RPP7. Adjacent HeLo-/HELL-domain encoding genes and NLR genes are found in many fungal genomes [82][83][84][85]. In addition, the mammalian NLR protein NLRP3 and its adaptor protein ASC interact in a very similar manner as HET-S and NWD2 do [86].…”

Section: Similarity Of Rpw8/hr To Fungal and Mammalian Immune Proteinsmentioning

confidence: 99%

RPW8/HR Repeats Predict NLR-dependent Hybrid Performance

Barragan

et al. 2019

Preprint

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Keywords RPW8, NLR, natural variation, autoimmunity, hybrid performance, MLKL, HET-S Barragan et al. RPW8/HR repeats and hybrid necrosis 2 SummaryHybrid offspring can look very different from their parents, including having greatly increased or decreased fitness. In many plant species, conflicts between divergent elements of the immune system can cause hybrids to express autoimmunity, a generally deleterious syndrome known as hybrid necrosis. We are investigating multiple hybrid necrosis cases in Arabidopsis thaliana that are caused by allele-specific interactions between different variants at two unlinked resistance (R) gene clusters. One is the RESISTANCE TO PERONOSPORA PARASITICA 7 (RPP7) cluster, which encodes an intracellular nucleotide binding site-leucine rich repeat (NLR) immune receptors that confer strain-specific resistance to oomycetes. The other is the RESISTANCE TO POWDERY MILDEW 8 (RPW8)/HOMOLOG OF RPW8 (HR) locus, which encodes atypical resistance proteins that can confer broad-spectrum resistance to filamentous pathogens. There is extensive structural variation in the RPW8/HR cluster, both at the level of gene copy number and at the level of C-terminal protein repeats of unknown function. We demonstrate that the number of RPW8/HR repeats correlate, albeit in a complex manner, with the severity of hybrid necrosis when these alleles are combined with specific RPP7 variants. This observation suggests that gross structural differences, rather than individual amino acid polymorphisms, guide the genetic interaction between RPW8/HR and RPP7 alleles. We discuss these findings in light of the similarity of RPW8/HR proteins with pore-forming toxins, MLKL and HET-S, from mammals and fungi.

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On the evolutionary trajectories of signal-transducing amyloids in fungi and beyond

Cited by 7 publications

References 34 publications

Structures of Pathological and Functional Amyloids and Prions, a Solid-State NMR Perspective

Structures of Pathological and Functional Amyloids and Prions, a Solid-State NMR Perspective

Functional Mammalian Amyloids and Amyloid-Like Proteins

RPW8/HR Repeats Predict NLR-dependent Hybrid Performance

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