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

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. Smith

Research output: Contribution to journalArticlepeer-review

37 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)890-898
Number of pages9
JournalNature Structural and Molecular Biology
Issue number10
StatePublished - Oct 1 2019

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Molecular Biology


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