HSPA8 hydrolyzes ATP to promote dissociation of the clathrin coat from the vesicle (reviewed in Sousa and Lafer, 2015). Interaction of HSPA8 with the C-terminal tail of clathrin may sterically block re-stabilization of the clathrin coat, which is thought to undergo transient cycles of 'breathing', or loosening of the interactions between the triskelions (Barouch et al, 1997; Rapoport et al, 2008; Xing et al, 2010). Alternately, HSPA8 may destabilize the clathrin coat through intermolecular collisions with the coat (reveiwed in Sousa and Lafer, 2015). The HSPA8-clathrin interaction persists once clathrin has been removed from the vesicle. This is thought to preclude aberrant repolymerization of clathrin by sequestering free clathrin (Schlossman et al, 1984; reviewed in Sousa and Lafer, 2015).