Clathrin has a distinctive three-pronged structure known as a triskelion. A triskelion consists of three clathrin heavy chains (CHC) and three clathrin light chains (CLC). In vitro, clathrin can self-assemble into empty polyhedral cages analogous to the polyhedral lattices that distinguish CCV.  Following are the view of clathrin and its assembly and disassembly including nucleation or initiation of coated pit formation (initiation); propagation of the clathrin lattice, accompanied by bilayer vesiculation and cargo recruitment (coat propagation); completion of the lattice and pinching off of the membrane vesicle (budding); transport or diffusion of the coated vesicle away from the membrane (traffic); and removal of the clathrin coat (uncoating). 
A network of interactions regulates clathrin coat formation, such as auxilin, amphyphysin, epsin, and AP180, contacting clathrin in what is turning out to be an extensive and complex network of interactions that control and modulate the formation of the clathrin coat. Perturbations of clathrin-dependent trafficking pathways have been associated with a variety of human diseases, as might be expected of processes fundamental to eukaryotic cell biology. Additionally, a wide variety of pathogens take advantage of clathrin-mediated endocytosis to enter cells and also co-opt clathrin machinery to promote other aspects of infection.


1.Myers MD,et al. Front Biosci (Landmark Ed). 2013 Jun 1;18:862-91.