Effect of clathrin light chains on the stiffness of clathrin lattices and membrane budding.

Clathrin-dependent transport processes require the polymerization of clathrin triskelia into polygonal scaffolds. Together with adapter proteins, clathrin collects cargo and induces membrane bud formation. It is not known to what extent clathrin light chains affect the structural and functional properties of clathrin lattices and the ability of clathrin to deform membranes.

Functional interaction of the auxilin J domain with the nucleotide- and substrate-binding modules of Hsc70.

The uncoating of clathrin-coated vesicles requires the DnaJ homologue auxilin for targeting Hsc70 to clathrin coats. This function involves a transient interaction of the auxilin J domain with Hsc70. We have now identified the structural elements of Hsc70 that are responsible for the uncoating activity, and we show that the hitherto accepted view, which implicates the 10-kDa carboxyl-terminal variable domain of Hsc70, is incorrect.

Mechanism of clathrin basket dissociation: separate functions of protein domains of the DnaJ homologue auxilin.

Auxilin was recently identified as cofactor for hsc70 in the uncoating of clathrin-coated vesicles (Ungewickell, E., H. Ungewickell, S.

Role of auxilin in uncoating clathrin-coated vesicles.

Clathrin-coated vesicles transport selected integral membrane proteins from the cell surface and the trans-Golgi network to the endosomal system. Before fusing with their target the vesicles must be stripped of their coats. This process is effected by the chaperone protein hsp70c together with a 100K cofactor which we here identify as the coat protein auxilin.

Bovine brain clathrin light chains impede heavy chain assembly in vitro.

Intact bovine brain clathrin triskelia, comprising three heavy and three light chains, require either 2 mM calcium or the assistance of protein co-factors for efficient assembly into regular cage structures (Keen, J. H., Willingham, M.