Complete reconstitution of clathrin basket formation with recombinant protein fragments: adaptor control of clathrin self-assembly.
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.
Greene
B
B
G.W. Hooper Foundation, Department of Microbiology and Immunology, and Departments of Biopharmaceutical Sciences and Pharmaceutical Chemistry, P.O. Box 0552, University of California, San Francisco, CA 94143, USA.
Liu
S H
SH
Wilde
A
A
Brodsky
F M
FM
D002966:Clathrin / Q000737:chemistry / Q000378:metabolism* / Q000648:ultrastructure; D004591:Electrophoresis, Polyacrylamide Gel; D008565:Membrane Proteins / Q000378:metabolism*; D008954:Models, Biological; D010446:Peptide Fragments / Q000378:metabolism* / Q000648:ultrastructure; D011108:Polymers / Q000378:metabolism*; D011485:Protein Binding; D020836:Protein Structure, Quaternary; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism / Q000648:ultrastructure
D002966:Clathrin; D008565:Membrane Proteins; D010446:Peptide Fragments; D011108:Polymers; D011994:Recombinant Proteins