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Cryo-EM of multiple cage architectures reveals a universal mode of clathrin self assembly

Research output: Contribution to journalArticle

  • Kyle L Morris
  • Joseph R Jones
  • Mary Halebian
  • Shenping Wu
  • Michael Baker
  • Jean-Paul Armache
  • Amaurys Avila Ibarra
  • Richard B Sessions
  • Alexander D Cameron
  • Yifan Cheng
  • Corinne J I Smith
Original languageEnglish
Pages (from-to)890 - 898
Number of pages14
JournalNature Structural and Molecular Biology
Volume26
DOIs
DateAccepted/In press - 2 Aug 2019
DatePublished (current) - 3 Oct 2019

Abstract

Clathrin forms diverse lattice and cage structures that change size and shape rapidly in response to the needs of eukaryotic cells during clathrin-mediated endocytosis and intracellular trafficking. We present the cryo-EM structure and molecular model of assembled porcine clathrin, providing insights into interactions that stabilize key elements of the clathrin lattice, namely, between adjacent heavy chains, at the light chain–heavy chain interface and within the trimerization domain. Furthermore, we report cryo-EM maps for five different clathrin cage architectures. Fitting structural models to three of these maps shows that their assembly requires only a limited range of triskelion leg conformations, yet inherent flexibility is required to maintain contacts. Analysis of the protein–protein interfaces shows remarkable conservation of contact sites despite architectural variation. These data reveal a universal mode of clathrin assembly that allows variable cage architecture and adaptation of coated vesicle size and shape during clathrin-mediated vesicular trafficking or endocytosis.

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    Rights statement: This is the author accepted manuscript (AAM). The final published version (version of record) is available online via Nature Research at https://www.nature.com/articles/s41594-019-0292-0#article-info . Please refer to any applicable terms of use of the publisher.

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