Clathrin self-assembly is mediated by a tandemly repeated superhelix

Joel A. Ybe, Frances M. Brodsky (), Kay Hofmann, Kai Lin, Shu-Hui Liu, Lin Chen, Thomas N. Earnest, Robert J. Fletterick and Peter K. Hwang
Additional contact information
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
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

Nature, 1999, vol. 399, issue 6734, 371-375

Abstract: 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.

Date: 1999
References: Add references at CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/20708 Abstract (text/html)
Access to the full text of the articles in this series is restricted.

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:399:y:1999:i:6734:d:10.1038_20708

Ordering information: This journal article can be ordered from
https://www.nature.com/

DOI: 10.1038/20708

Access Statistics for this article

Nature is currently edited by Magdalena Skipper

More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().