A novel form of collective mesenchymal cell migration is identified during chick gastrulation, where a dynamic 3D meshwork supported by N-cadherin-mediated adhesion coordinates movement and enhances directional migration in the unconfined space between ectoderm and endoderm.
Protein–protein interactions and localization dependencies between septin cytoskeleton and the exocyst complex using the fission yeast model system reveal one of the most conserved functions of septins in exocytosis.
Full-length, autoinhibited LRRK2 assembles into distinct, shorter microtubule-bound filaments via a previously unobserved N-terminal repeat interface, revealing new structural states with potential therapeutic implications.
