[2] Barbara Pearse named the protein clathrin at the suggestion of Graeme Mitchison, selecting it from three possible options.

[3] Coat-proteins, like clathrin, are used to build small vesicles in order to transport molecules within cells.

The endocytosis and exocytosis of vesicles allows cells to communicate, to transfer nutrients, to import signaling receptors, to mediate an immune response after sampling the extracellular world, and to clean up the cell debris left by tissue inflammation.

The endocytic pathway can be hijacked by viruses and other pathogens in order to gain entry to the cell during infection.

The main clathrin heavy chain, located on chromosome 17 in humans, is found in all cells.

This triskelion will bind to other membrane-attached triskelia to form a rounded lattice of hexagons and pentagons, reminiscent of the panels on a soccer ball, that pulls the membrane into a bud.

In a cell, a triskelion floating in the cytoplasm binds to an adaptor protein, linking one of its feet to the membrane at a time.

The stabilization of kinetochore fibers requires the trimeric structure of clathrin in order to crosslink microtubules.

[11][12][13] Clathrin-mediated endocytosis (CME) regulates many cellular physiological processes such as the internalization of growth factors and receptors, entry of pathogens, and synaptic transmission.

It is believed that cellular invaders use the nutrient pathway to gain access to a cell's replicating mechanisms.

These two compounds selectively block the endocytic ligand association with the clathrin terminal domain in vitro.