Molecular architecture of the complete COG tethering complex

Nat Struct Mol Biol. 2016 Aug;23(8):758-60. doi: 10.1038/nsmb.3263. Epub 2016 Jul 18.

Abstract

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.

MeSH terms

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

Substances

  • Adaptor Proteins, Vesicular Transport
  • Multiprotein Complexes
  • Saccharomyces cerevisiae Proteins