Liquid-liquid phase separation of tau is demonstrated to be an equilibrium state, stable only within a narrow range near physiological conditions, and thus has the capacity to regulate biological processes.
A novel auto-inhibitory mechanism regulates the functional activity of the cellular prion protein, PrPC, providing for the first time a coherent molecular model for both its pathological and physiological effects.
A novel regulatory cascade downstream of Tau and spectraplakins ensures that synaptic proteins are delivered to axonal terminals in the developing and ageing brain, providing potential explanations for precocious synapse loss in dementias.
Tau monomer from aggregate-containing cell models and tauopathy brains adopts discrete structures that act as templates, dictating the conformation of distinct strains that result from its seeding activity.
In keratinocytes, the BRAF and RAF1 proteins work independently to balance the activity of mitogenic and stress kinase cascades and uphold the mechanical and immunological barrier functions of the epidermis.
Cryo-EM structures of heparin-induced tau filaments differ from those observed in neurodegenerative disease, illustrating their structural versatility, and prompting questions about the relevance of in vitro amyloid models.