Eileen M. Lafer

The paper shows that balancing actin filament nucleation and elongation is necessary to deform protein condensates into high aspect ratio structures.

This study shows clathrin accessory proteins destabilize protein condensates while promoting clathrin lattice assembly and exclusion, revealing a mechanism linking phase separation to endocytosis.

This study designs intrinsically disordered ligands that control receptor uptake via endocytosis by modulating their sequence to promote or hinder internalization.

This study shows that protein condensates and clathrin assembly regulate each other during clathrin-mediated endocytosis, enhancing vesicle formation while controlling condensate growth.

This study shows Epsin1 stabilizes initiator protein condensation during clathrin-mediated endocytosis only when ubiquitin is present, ensuring cargo-specific vesicle formation.

The paper shows that actin-binding proteins forming liquid-like condensates can polymerize and bundle actin filaments, expanding the known set of proteins capable of this function.

This study shows clathrin is a strong membrane curvature sensor, with its sensitivity amplified by adaptor proteins, highlighting the role of protein networks in curvature sensing.

This paper shows that excess α-synuclein impairs synaptic vesicle recycling by sequestering Hsc70, and that increasing Hsc70 levels can reverse this defect in a vertebrate synapse.