Molecular architecture of the complete COG tethering complex

Jun Yong Ha, Hui-Ting Chou, Daniel Ungar, Calvin K Yip, Thomas Walz, Frederick M Hughson

Research output: Contribution to journalArticlepeer-review


The conserved oligomeric Golgi (COG) complex orchestrates vesicular trafficking to and within the Golgi apparatus. Here, we use negative-stain electron microscopy to elucidate the architecture of the hetero-octameric COG complex from Saccharomyces cerevisiae. Intact COG has an intricate shape, with four (or possibly five) flexible legs, that differs strikingly from that of the exocyst complex and appears to be well suited for vesicle capture and fusion.
Original languageEnglish
Pages (from-to)758-760
Number of pages3
JournalNature Structural & Molecular Biology
Publication statusPublished - 18 Jul 2016

Bibliographical note

This is an author-produced version of the published paper. Uploaded in accordance with the publisher’s self-archiving policy. Further copying may not be permitted; contact the publisher for details. Embargo period: 6 months [paper and supplementary file]


  • Adaptor Proteins, Vesicular Transport/ultrastructure
  • Golgi Apparatus/ultrastructure
  • Microscopy, Electron
  • Multiprotein Complexes/ultrastructure
  • Protein Structure, Quaternary
  • Saccharomyces cerevisiae Proteins/ultrastructure
  • Saccharomyces cerevisiae/ultrastructure

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