Complete reconstitution of clathrin basket formation with recombinant protein fragments: adaptor control of clathrin self-assembly

Traffic. 2000 Jan;1(1):69-75. doi: 10.1034/j.1600-0854.2000.010110.x.

Abstract

Clathrin polymerization into a polyhedral basket, surrounding budding membrane vesicles, mediates protein sorting during endocytosis and organelle biogenesis. Adaptor proteins target clathrin assembly to specific membrane sites and sequester receptors into the clathrin coat. We have reconstituted complete clathrin basket formation from recombinantly expressed fragments of clathrin and adaptors. This reconstitution reveals a hierarchy of clathrin self-assembly interactions and demonstrates that adaptors control basket formation by alignment of the distal domains of the clathrin triskelion leg through their binding to the terminal domain.

Publication types

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

MeSH terms

  • Clathrin / chemistry
  • Clathrin / metabolism*
  • Clathrin / ultrastructure
  • Electrophoresis, Polyacrylamide Gel
  • Membrane Proteins / metabolism*
  • Models, Biological
  • Peptide Fragments / metabolism*
  • Peptide Fragments / ultrastructure
  • Polymers / metabolism*
  • Protein Binding
  • Protein Structure, Quaternary
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / metabolism
  • Recombinant Proteins / ultrastructure

Substances

  • Clathrin
  • Membrane Proteins
  • Peptide Fragments
  • Polymers
  • Recombinant Proteins