Using a microtubule-binding fragment of the full-length tau protein, Frost and colleagues demonstrate that tau can assume multiple conformations that can be seeded and faithfully propagated in vitro. The findings may help to explain the structural diversity of tau filaments in vivo, as well as the clinico-pathologic diversity of the tauopathies. Importantly, the paper expands the growing list of protein assemblies that can exist as polymorphic and polyfunctional strains.
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Emory University
Using a microtubule-binding fragment of the full-length tau protein, Frost and colleagues demonstrate that tau can assume multiple conformations that can be seeded and faithfully propagated in vitro. The findings may help to explain the structural diversity of tau filaments in vivo, as well as the clinico-pathologic diversity of the tauopathies. Importantly, the paper expands the growing list of protein assemblies that can exist as polymorphic and polyfunctional strains.
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