Clathrin uncoating reaction

Another activity associated with a stress-70 protein is the in vitro disassembly of clathrin cages into triskelions (see Section I V,D). Rothman and colleagues isolated and characterized a protein from bovine brain that facilitated the disassembly of clathrin cages in a reaction that required hydrolysis of ATP they referred to the protein as a clathrin-uncoating ATPase (Schlossman et ai, 1984). Subsequently, it was realized that this protein was a constitutively expressed member of the stress-70 family (HSC70) (Chappell et al 1986). 

Heuser, J., and Steer, C. J. (1989). Trimeric binding of the 70-kD uncoating ATPase to the vertices of clathrin triskelia A candidate intermediate in the vesicle uncoating reaction. J. Cell Biol. 109, 1457-1466. 

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