Large self-assembled clathrin lattices spontaneously disassemble without sufficient adaptor proteins
Fig 1
The structure-resolved reaction-diffusion model for clathrin recruitment and assembly on membranes captures structure, valency, and excluded volume.
Clathrin trimers are initialized in solution, but bind to adaptor proteins that are localized to the surface. Clathrin binds to adaptors only after the adaptors have localized to the surface, which is consistent with the behavior of the adaptor AP-2[16]. Adaptor proteins can bind specific lipids on the membrane surface when initialized in solution. Clathrin-clathrin sites and clathrin-adaptor sites exclude one another with a radius of σ = 5nm (blue circles) and σ = 1nm, respectively, but only when they are unbound; bound sites do not exclude volume. Therefore, at all times in the simulation, center-of-mass (COM) sites on trimers exclude other trimer COMs at σ = 10nm (purple circles), to ensure the lattices do not overlap with one another.