Folding and trimerization of clathrin subunits at the triskelion hub

Inke S. Näthke, John Heuser, Andrei Lupas, Jeff Stock, Christoph W. Turck, Frances M. Brodsky

Research output: Contribution to journalArticle

127 Scopus citations

Abstract

The triskelion shape of the clathrin molecule enables it to form the polyhedral protein network that covers clathrin-coated pits and vesicles. Domains within the clathrin heavy chain that are responsible for maintaining triskelion shape and function were identified and localized. Sequences that mediate trimerization are distal to the carboxyl terminus and are adjacent to a domain that mediates both light chain binding and clathrin assembly. Structural modeling predicts that within this domain, the region of heavy chain-light chain interaction is a bundle of three or four α helices. These studies establish a low resolution model of clathrin subunit folding in the central portion (hub) of the triskelion, thus providing a basis for future mutagenesis experiments.

Original languageEnglish (US)
Pages (from-to)899-910
Number of pages12
JournalCell
Volume68
Issue number5
DOIs
StatePublished - Mar 6 1992

All Science Journal Classification (ASJC) codes

  • Biochemistry, Genetics and Molecular Biology(all)

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    Näthke, I. S., Heuser, J., Lupas, A., Stock, J., Turck, C. W., & Brodsky, F. M. (1992). Folding and trimerization of clathrin subunits at the triskelion hub. Cell, 68(5), 899-910. https://doi.org/10.1016/0092-8674(92)90033-9