Regulation of clathrin assembly and trimerization defined using recombinant triskelion hubs

Cell. 1995 Oct 20;83(2):257-67. doi: 10.1016/0092-8674(95)90167-1.


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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Cattle
  • Clathrin / chemistry*
  • Clathrin / genetics
  • Clathrin / metabolism
  • Clathrin / ultrastructure
  • Escherichia coli / genetics
  • Eye Proteins / chemistry
  • Eye Proteins / genetics
  • Eye Proteins / metabolism
  • Eye Proteins / ultrastructure
  • Humans
  • Models, Molecular
  • Molecular Sequence Data
  • Peptide Fragments / chemistry
  • Peptide Fragments / genetics
  • Peptide Fragments / metabolism
  • Protein Conformation
  • Protein Folding
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / metabolism
  • Structure-Activity Relationship


  • Clathrin
  • Eye Proteins
  • Peptide Fragments
  • Recombinant Proteins

Associated data

  • GENBANK/U31757