Brain clathrin and clathrin-associated proteins.

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Abstract
The assembly of clathrin into baskets or cages in vitro may depend on formation of a complex between clathrin and a polypeptide doublet migrating in the 30,000-MW region. Clathrin with several associated proteins was isolated from coated-vesicle fractions of bovine cerebral cortex. Most associated proteins were separated by Sepharose 4B column chromatography. The eluted clathrin retained only the 30,000-MW doublet and assembled into baskets at pH 6.5. Limited proteolysis of coated vesicles or clathrin assembled as baskets removed these clathrin-associated proteins (CAP) without detectably altering clathrin. Enzyme[chymotrypsin]-treated clathrin assembled into open-lattice structures but no longer formed baskets in vitro. Latex particles with bound enzyme cleaved the CAP from coated vesicles and clathrin baskets, suggesting that the CAP protrude from the exterior of the clathrin lattice.