作者: Andrey V. Kajava , Karsten Klopffleisch , Shuhua Chen , Kay Hofmann
DOI: 10.1038/SREP07436
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摘要: The Rip homotypic interaction motif (RHIM) is a short, non-globular sequence stretch that mediates key of mammalian necroptosis signaling. In order to understand its unusual oligomerization properties, we set out trace the evolutionary origins RHIM by identifying distantly related protein motifs might employ same binding mode. was found be prion-forming domain HET-s protein, which oligomerizes forming structurally well-characterized fibrils and involved in fungal heterokaryon incompatibility. This relationship explains recently reported propensity form amyloid fibrils, but suggests these have different structural architecture than currently assumed. These findings, together with numerous observations RHIM-like immunity proteins from wide range species, provide insight modern innate pathways animals, plants fungi.