Author
Listed:
- Joel A. Ybe
(G. W. Hooper Foundation)
- Frances M. Brodsky
(G. W. Hooper Foundation)
- Kay Hofmann
(Bioinformatics Group, MEMOREC Stoffel GmbH)
- Kai Lin
(University of California San Francisco
University of Massachusetts Medical Center)
- Shu-Hui Liu
(G. W. Hooper Foundation)
- Lin Chen
(G. W. Hooper Foundation)
- Thomas N. Earnest
(Macromolecular Cyrstallography Facility at the Advanced Light Source, Lawrence Berkeley National Laboraotry)
- Robert J. Fletterick
(University of California San Francisco)
- Peter K. Hwang
(University of California San Francisco)
Abstract
Clathrin is a triskelion-shaped cytoplasmic protein that polymerizes into a polyhedral lattice on intracellular membranes to form protein-coated membrane vesicles. Lattice formation induces the sorting of membrane proteins during endocytosis and organelle biogenesis by interacting with membrane-associated adaptor molecules1. The clathrin triskelion is a trimer of heavy-chain subunits (1,675 residues), each binding a single light-chain subunit, in the hub domain (residues 1,074–1,675). Light chains negatively modulate polymerization so that intracellular clathrin assembly is adaptor-dependent2. Here we report the atomic structure, to 2.6 Å resolution, of hub residues 1,210–1,516 involved in mediating spontaneous clathrin heavy-chain polymerization and light-chain association3,4. The hub fragment folds into an elongated coil of α-helices, and alignment analyses reveal a 145-residue motif that is repeated seven times along the filamentous leg and appears in other proteins involved in vacuolar protein sorting. The resulting model provides a three-dimensional framework for understanding clathrin heavy-chain self-assembly, light-chain binding and trimerization.
Suggested Citation
Joel A. Ybe & Frances M. Brodsky & Kay Hofmann & Kai Lin & Shu-Hui Liu & Lin Chen & Thomas N. Earnest & Robert J. Fletterick & Peter K. Hwang, 1999.
"Clathrin self-assembly is mediated by a tandemly repeated superhelix,"
Nature, Nature, vol. 399(6734), pages 371-375, May.
Handle:
RePEc:nat:nature:v:399:y:1999:i:6734:d:10.1038_20708
DOI: 10.1038/20708
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