Brandon T. Malady

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 shows reflectin proteins form liquid-liquid phase-separated condensates that mirror spatial organization in squid skin Bragg lamellae, controlled by charge density and protein proportions.

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.

This study shows that charge screening and hydrophobicity drive the assembly and liquid-liquid phase separation of reflectin proteins, revealing mechanisms for tunable reflectivity in squid.

This paper shows that ubiquitin stabilizes Eps15 condensates, which are essential for clathrin-mediated endocytosis, and that ubiquitylation regulates the dynamics of endocytic assemblies.

This study shows that charge neutralization, not aromatic content, drives the assembly and fine-tuning of reflectin-based Bragg reflectors in squid skin cells.