To selectively internalize proteins into the endosomal system, eukaryotic cells rely on clathrin adaptors such as the clathrin assembly lymphoid myeloid leukaemia protein (CALM), but details regarding the underlying mechanism remain unexplored. Here, the authors characterize the effect of CALM on lipid packaging density and membrane remodelling through a combination of in vitro studies, neutron reflectometry, grazing incidence X-ray diffraction, atomic force microscopy and solid-state nuclear magnetic resonance, and show that CALM’s amphiphilic N-terminal helix embeds into the membrane to stabilize protein docking.
- Andreas Santamaria
- Daniel Pereira
- Armando Maestro
