Molecular architecture of the complete COG tethering complex. Author Jun Ha, Hui-Ting Chou, Daniel Ungar, Calvin Yip, Thomas Walz, Frederick Hughson Publication Year 2016 Type Journal Article 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. Keywords Multiprotein Complexes, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Golgi Apparatus, Protein Structure, Quaternary, Adaptor Proteins, Vesicular Transport, Microscopy, Electron Journal Nat Struct Mol Biol Volume 23 Issue 8 Pages 758-60 Date Published 2016 Aug ISSN Number 1545-9985 DOI 10.1038/nsmb.3263 Alternate Journal Nat Struct Mol Biol PMCID PMC4972656 PMID 27428773 PubMedPubMed CentralGoogle ScholarBibTeXEndNote X3 XML