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    Cell. 1995 Oct 20;83(2):257-67.

    Regulation of clathrin assembly and trimerization defined using recombinant triskelion hubs.

    Liu SH, Wong ML, Craik CS, Brodsky FM.

    Department of Pharmacy, School of Pharmacy, University of California, San Francisco 94143-0552, USA.

    Clathrin polymerization into a polyhedral vesicle coat drives receptor sorting at cellular membranes during endocytosis and organelle biogenesis. To study clathrin self-assembly, we expressed the C-terminal third of the clathrin heavy chain in bacteria. The recombinant fragment trimerized, bound clathrin light chains, and morphologically resembled the hub domain of the triskelion-shaped clathrin molecule. Self-assembly of recombinant hubs demonstrated a regulatory role for clathrin light chains and for the distal portions of triskelion legs in clathrin coat formation. Deletion mutagenesis of the hub localized a domain mediating light chain binding and clathrin self-assembly and mapped a transferable trimerization domain. These studies define molecular interactions controlling clathrin self-assembly and establish a recombinant system for future analysis.

    PMID: 7585943 [PubMed - indexed for MEDLINE]

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