Kurtin, D. | bioRxiv Science

bioRxiv2025

A universal dynamic routing architecture governs the flow of human cortical activity

Behaviour requires distributed neural processing to be flexibly integrated and segregated, which in turn demands that information be dynamically routed across the brain. However, whether a unifying principle governs the routing of neural activity remains unknown. Here, we report that the flow of cortical activity is directed through canonical routing modes that are conserved across individuals, robust to variations in age, frequency band, brain state, and even the presence of neurodegeneration. These modes are constructed from the divergence and vorticity of the time-varying unit-phase vector field derived from electroencephalogram (EEG) recordings. We show that the canonical routing modes are flexibly combined to generate distinct, state- and function-dependent flow architectures that remain consistent across individuals. Disruption to the routing mode dynamics mechanistically links structural abnormalities and cognitive impairment in Alzheimers disease. Together, these canonical routing modes provide a unified framework for describing, modelling, and predicting the dynamic integration and segregation of macroscopic brain activity underpinning behaviour.

neuroscience↗

bioRxiv2020

The structures of natively assembled clathrin coated vesicles

Vesicle trafficking by clathrin coated vesicles (CCVs) is one of the major mechanisms by which proteins and nutrients are absorbed by the cell and transported between organelles. The individual proteins comprising the coated vesicles include clathrin heavy chain, clathrin light chain, and a variety of adaptor protein complexes. Much is known about the structures of the individual CCV components, but data are lacking about the structures of the fully assembled complexes together with membrane and in complex with cargo. Here we determined the structures of natively assembled CCVs in a variety of geometries. We show that the adaptor {beta}2-appendages crosslink adjacent CHC {beta}-propellers and that the appendage densities reside almost exclusively in CCV hexagonal faces. We resolve how AP2 and other associated factors in hexagonal faces form an assembly hub with an extensive web of interactions between neighboring {beta}-propellers and propose a structural model that explains how adaptor binding can direct the formation of pentagonal and hexagonal faces.

biophysics↗