Molecular architecture of the complete COG tethering complex.

TitleMolecular architecture of the complete COG tethering complex.
Publication TypeJournal Article
Year of Publication2016
AuthorsHa, JYong, Chou, H-T, Ungar, D, Yip, CK, Walz, T, Hughson, FM
JournalNat Struct Mol Biol
Date Published2016 Aug
KeywordsAdaptor Proteins, Vesicular Transport, Golgi Apparatus, Microscopy, Electron, Multiprotein Complexes, Protein Structure, Quaternary, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins

<p>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.</p>

Alternate JournalNat Struct Mol Biol
PubMed ID27428773
PubMed Central IDPMC4972656
Grant ListP01 GM062580 / GM / NIGMS NIH HHS / United States
R01 GM071574 / GM / NIGMS NIH HHS / United States