Title | Molecular architecture of the complete COG tethering complex. |
Publication Type | Journal Article |
Year of Publication | 2016 |
Authors | Ha, JYong, Chou, H-T, Ungar, D, Yip, CK, Walz, T, Hughson, FM |
Journal | Nat Struct Mol Biol |
Volume | 23 |
Issue | 8 |
Pagination | 758-60 |
Date Published | 2016 Aug |
ISSN | 1545-9985 |
Keywords | Adaptor Proteins, Vesicular Transport, Golgi Apparatus, Microscopy, Electron, Multiprotein Complexes, Protein Structure, Quaternary, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins |
Abstract | <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> |
DOI | 10.1038/nsmb.3263 |
Alternate Journal | Nat Struct Mol Biol |
PubMed ID | 27428773 |
PubMed Central ID | PMC4972656 |
Grant List | P01 GM062580 / GM / NIGMS NIH HHS / United States R01 GM071574 / GM / NIGMS NIH HHS / United States |