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- Title
Clathrin self-assembly is mediated by a tandemly repeated superhelix.
- Authors
Ybe, J A; Brodsky, F M; Hofmann, K; Lin, K; Liu, S H; Chen, L; Earnest, T N; Fletterick, R J; Hwang, P K
- 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 molecules. 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-dependent. Here we report the atomic structure, to 2.6 A resolution, of hub residues 1,210-1,516 involved in mediating spontaneous clathrin heavy-chain polymerization and light-chain association. The hub fragment folds into an elongated coil of alpha-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.
- Publication
Nature, 1999, Vol 399, Issue 6734, p371
- ISSN
0028-0836
- Publication type
Journal Article
- DOI
10.1038/20708