Enzymatic dissociation of clathrin cages in a two-stage process - PubMed (original) (raw)

. 1985 Aug 25;260(18):10044-9.

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Enzymatic dissociation of clathrin cages in a two-stage process

S L Schmid et al. J Biol Chem. 1985.

Free article

Abstract

Uncoating ATPase catalyzes the ATP-dependent dissociation of clathrin from coated vesicles and empty cages. Following an uncoating reaction, clathrin triskelions are released intact, in a stoichiometric complex with bound uncoating protein. This overall uncoating process was dissected into two partial reactions. In the first, ATP hydrolysis drives the transient displacement of a portion of a triskelion from a cage. Uncoating protein then captures the displaced triskelion, in the second stage, by binding to a newly exposed site on clathrin that had previously been buried in the cage lattice. Triskelion-uncoating protein complexes are released when all points of attachment of the triskelion to the cage have been severed. The uncoating protein interacts with a distinct site on clathrin for each of these reactions.

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