@article{2862, keywords = {Multiprotein Complexes, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Golgi Apparatus, Protein Structure, Quaternary, Adaptor Proteins, Vesicular Transport, Microscopy, Electron}, author = {Jun Ha and Hui-Ting Chou and Daniel Ungar and Calvin Yip and Thomas Walz and Frederick Hughson}, title = {Molecular architecture of the complete COG tethering complex.}, 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.
}, year = {2016}, journal = {Nat Struct Mol Biol}, volume = {23}, pages = {758-60}, month = {2016 Aug}, issn = {1545-9985}, doi = {10.1038/nsmb.3263}, language = {eng}, }