David J. Owen

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

This study determines the structure of the COPI vesicle coat with GOLPH3 and shows how it preferentially binds Golgi residents at late cisternae through coincidence detection of COPI and lipid.

This study identifies RABGAP1 as a sensor that modulates APP trafficking and processing by regulating RAB activity on endosomal subdomains, with implications for Alzheimer's disease.

This study uses biophysical methods to analyze AP2 interactions with biomimetic membranes, revealing insights into clathrin-mediated endocytosis mechanisms.

This study uses biophysical methods to show how CALM interacts with PtdIns(4,5)P2-containing membranes, revealing structural details of its membrane binding and curvature induction mechanism.

The paper identifies a mechanism by which TBC1D23 recognizes transport vesicles destined for the Golgi through direct binding to a shared cargo motif.

The paper elucidates the structural basis of retromer core trimer assembly with SNX3, showing how it forms tubular carriers and incorporates cargo through conserved interfaces linked to Parkinson's disease mutations.

The paper determines the structure and interactions of AP2 and clathrin during clathrin-coated vesicle formation using cryo-EM and tomography.